Entry euk:AFG32_HUMAN

ID   AFG32_HUMAN             Reviewed;         797 AA.
AC   Q9Y4W6; Q6P1L0;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   12-APR-2017, entry version 168.
DE   RecName: Full=AFG3-like protein 2;
DE            EC=3.4.24.- {ECO:0000269|PubMed:14623864};
DE   AltName: Full=Paraplegin-like protein;
GN   Name=AFG3L2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=10395799; DOI=10.1006/geno.1999.5818;
RA   Banfi S., Bassi M.T., Andolfi G., Marchitiello A., Zanotta S.,
RA   Ballabio A., Casari G., Franco B.;
RT   "Identification and characterization of AFG3L2, a novel paraplegin-
RT   related gene.";
RL   Genomics 59:51-58(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH SPG7.
RX   PubMed=14623864; DOI=10.1083/jcb.200304112;
RA   Atorino L., Silvestri L., Koppen M., Cassina L., Ballabio A.,
RA   Marconi R., Langer T., Casari G.;
RT   "Loss of m-AAA protease in mitochondria causes complex I deficiency
RT   and increased sensitivity to oxidative stress in hereditary spastic
RT   paraplegia.";
RL   J. Cell Biol. 163:777-787(2003).
RN   [4]
RP   SUBUNIT.
RX   PubMed=17101804; DOI=10.1128/MCB.01470-06;
RA   Koppen M., Metodiev M.D., Casari G., Rugarli E.I., Langer T.;
RT   "Variable and tissue-specific subunit composition of mitochondrial m-
RT   AAA protease complexes linked to hereditary spastic paraplegia.";
RL   Mol. Cell. Biol. 27:758-767(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [8]
RP   INTERACTION WITH MAIP1.
RX   PubMed=27499296; DOI=10.1016/j.molcel.2016.06.033;
RA   Floyd B.J., Wilkerson E.M., Veling M.T., Minogue C.E., Xia C.,
RA   Beebe E.T., Wrobel R.L., Cho H., Kremer L.S., Alston C.L.,
RA   Gromek K.A., Dolan B.K., Ulbrich A., Stefely J.A., Bohl S.L.,
RA   Werner K.M., Jochem A., Westphall M.S., Rensvold J.W., Taylor R.W.,
RA   Prokisch H., Kim J.J., Coon J.J., Pagliarini D.J.;
RT   "Mitochondrial protein interaction mapping identifies regulators of
RT   respiratory chain function.";
RL   Mol. Cell 63:621-632(2016).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH MAIP1.
RX   PubMed=27642048; DOI=10.1016/j.molcel.2016.08.020;
RA   Koenig T., Troeder S.E., Bakka K., Korwitz A., Richter-Dennerlein R.,
RA   Lampe P.A., Patron M., Muehlmeister M., Guerrero-Castillo S.,
RA   Brandt U., Decker T., Lauria I., Paggio A., Rizzuto R., Rugarli E.I.,
RA   De Stefani D., Langer T.;
RT   "The m-AAA protease associated with neurodegeneration limits MCU
RT   activity in mitochondria.";
RL   Mol. Cell 64:148-162(2016).
RN   [10]
RP   STRUCTURE BY NMR OF 164-251.
RG   Northeast structural genomics consortium (NESG);
RT   "Northeast structural genomics consortium target HR6741A.";
RL   Submitted (MAR-2012) to the PDB data bank.
RN   [11]
RP   VARIANT SCA28 LYS-700.
RX   PubMed=20354562; DOI=10.1038/ejhg.2010.40;
RA   Edener U., Wollner J., Hehr U., Kohl Z., Schilling S., Kreuz F.,
RA   Bauer P., Bernard V., Gillessen-Kaesbach G., Zuhlke C.;
RT   "Early onset and slow progression of SCA28, a rare dominant ataxia in
RT   a large four-generation family with a novel AFG3L2 mutation.";
RL   Eur. J. Hum. Genet. 18:965-968(2010).
RN   [12]
RP   VARIANTS SCA28 ILE-654; VAL-666; ARG-666; THR-666; ARG-671 AND
RP   GLU-671.
RX   PubMed=20725928; DOI=10.1002/humu.21342;
RA   Cagnoli C., Stevanin G., Brussino A., Barberis M., Mancini C.,
RA   Margolis R.L., Holmes S.E., Nobili M., Forlani S., Padovan S.,
RA   Pappi P., Zaros C., Leber I., Ribai P., Pugliese L., Assalto C.,
RA   Brice A., Migone N., Durr A., Brusco A.;
RT   "Missense mutations in the AFG3L2 proteolytic domain account for
RT   approximately 1.5% of European autosomal dominant cerebellar
RT   ataxias.";
RL   Hum. Mutat. 31:1117-1124(2010).
RN   [13]
RP   VARIANTS SCA28 THR-432; LYS-691; GLU-694 AND GLN-702, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=20208537; DOI=10.1038/ng.544;
RA   Di Bella D., Lazzaro F., Brusco A., Plumari M., Battaglia G.,
RA   Pastore A., Finardi A., Cagnoli C., Tempia F., Frontali M.,
RA   Veneziano L., Sacco T., Boda E., Brussino A., Bonn F., Castellotti B.,
RA   Baratta S., Mariotti C., Gellera C., Fracasso V., Magri S., Langer T.,
RA   Plevani P., Di Donato S., Muzi-Falconi M., Taroni F.;
RT   "Mutations in the mitochondrial protease gene AFG3L2 cause dominant
RT   hereditary ataxia SCA28.";
RL   Nat. Genet. 42:313-321(2010).
RN   [14]
RP   VARIANT SPAX5 CYS-616, AND CHARACTERIZATION OF VARIANT SPAX5 CYS-616.
RX   PubMed=22022284; DOI=10.1371/journal.pgen.1002325;
RA   Pierson T.M., Adams D., Bonn F., Martinelli P., Cherukuri P.F.,
RA   Teer J.K., Hansen N.F., Cruz P., Mullikin J.C., Blakesley R.W.,
RA   Golas G., Kwan J., Sandler A., Fuentes Fajardo K., Markello T.,
RA   Tifft C., Blackstone C., Rugarli E.I., Langer T., Gahl W.A., Toro C.;
RT   "Whole-exome sequencing identifies homozygous AFG3L2 mutations in a
RT   spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA
RT   proteases.";
RL   PLoS Genet. 7:E1002325-E1002325(2011).
RN   [15]
RP   VARIANT SCA28 HIS-689.
RX   PubMed=24293060; DOI=10.1007/s12031-013-0187-1;
RA   Loebbe A.M., Kang J.S., Hilker R., Hackstein H., Mueller U., Nolte D.;
RT   "A novel missense mutation in AFG3L2 associated with late onset and
RT   slow progression of spinocerebellar ataxia type 28.";
RL   J. Mol. Neurosci. 52:493-496(2014).
RN   [16]
RP   VARIANT SCA28 ASN-689.
RX   PubMed=26677414; DOI=10.1186/s40673-015-0038-7;
RA   Zuehlke C., Mikat B., Timmann D., Wieczorek D., Gillessen-Kaesbach G.,
RA   Buerk K.;
RT   "Spinocerebellar ataxia 28: a novel AFG3L2 mutation in a German family
RT   with young onset, slow progression and saccadic slowing.";
RL   Cerebellum Ataxias 2:19-19(2015).
CC   -!- FUNCTION: ATP-dependent protease which is essential for axonal and
CC       neuron development. In neurons, mediates degradation of SMDT1/EMRE
CC       before its assembly with the uniporter complex, limiting the
CC       availability of SMDT1/EMRE for MCU assembly and promoting
CC       efficient assembly of gatekeeper subunits with MCU.
CC       {ECO:0000269|PubMed:27642048}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9WZ49};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9WZ49};
CC   -!- SUBUNIT: Homooligomer (PubMed:17101804). Interacts with SPG7; the
CC       interaction is required for the efficient assembly of
CC       mitochondrial complex I (PubMed:14623864). Interacts with MAIP1
CC       (PubMed:27499296, PubMed:27642048). {ECO:0000269|PubMed:14623864,
CC       ECO:0000269|PubMed:17101804, ECO:0000269|PubMed:27499296,
CC       ECO:0000269|PubMed:27642048}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000269|PubMed:10395799}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:10395799}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the cerebellar
CC       Purkinje cells. {ECO:0000269|PubMed:20208537}.
CC   -!- DISEASE: Spinocerebellar ataxia 28 (SCA28) [MIM:610246]:
CC       Spinocerebellar ataxia is a clinically and genetically
CC       heterogeneous group of cerebellar disorders. Patients show
CC       progressive incoordination of gait and often poor coordination of
CC       hands, speech and eye movements, due to degeneration of the
CC       cerebellum with variable involvement of the brainstem and spinal
CC       cord. SCA28 is an autosomal dominant cerebellar ataxia (ADCA) with
CC       a slow progressive course and no evidence of sensory involvement
CC       or cognitive impairment. {ECO:0000269|PubMed:20208537,
CC       ECO:0000269|PubMed:20354562, ECO:0000269|PubMed:20725928,
CC       ECO:0000269|PubMed:24293060, ECO:0000269|PubMed:26677414}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Spastic ataxia 5, autosomal recessive (SPAX5)
CC       [MIM:614487]: A neurodegenerative disorder characterized by early
CC       onset spasticity, peripheral neuropathy, ptosis, oculomotor
CC       apraxia, dystonia, cerebellar atrophy, and progressive myoclonic
CC       epilepsy. {ECO:0000269|PubMed:22022284}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase
CC       M41 family. {ECO:0000305}.
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DR   EMBL; Y18314; CAB48398.1; -; mRNA.
DR   EMBL; BC065016; AAH65016.1; -; mRNA.
DR   CCDS; CCDS11859.1; -.
DR   RefSeq; NP_006787.2; NM_006796.2.
DR   UniGene; Hs.726355; -.
DR   PDB; 2LNA; NMR; -; A=164-251.
DR   PDBsum; 2LNA; -.
DR   ProteinModelPortal; Q9Y4W6; -.
DR   SMR; Q9Y4W6; -.
DR   BioGrid; 116139; 64.
DR   IntAct; Q9Y4W6; 46.
DR   MINT; MINT-1161944; -.
DR   STRING; 9606.ENSP00000269143; -.
DR   DrugBank; DB00171; Adenosine triphosphate.
DR   MEROPS; M41.007; -.
DR   iPTMnet; Q9Y4W6; -.
DR   PhosphoSitePlus; Q9Y4W6; -.
DR   SwissPalm; Q9Y4W6; -.
DR   BioMuta; AFG3L2; -.
DR   DMDM; 126302516; -.
DR   EPD; Q9Y4W6; -.
DR   MaxQB; Q9Y4W6; -.
DR   PaxDb; Q9Y4W6; -.
DR   PeptideAtlas; Q9Y4W6; -.
DR   PRIDE; Q9Y4W6; -.
DR   TopDownProteomics; Q9Y4W6; -.
DR   Ensembl; ENST00000269143; ENSP00000269143; ENSG00000141385.
DR   GeneID; 10939; -.
DR   KEGG; hsa:10939; -.
DR   UCSC; uc002kqz.3; human.
DR   CTD; 10939; -.
DR   DisGeNET; 10939; -.
DR   GeneCards; AFG3L2; -.
DR   GeneReviews; AFG3L2; -.
DR   H-InvDB; HIX0027367; -.
DR   HGNC; HGNC:315; AFG3L2.
DR   HPA; HPA004479; -.
DR   HPA; HPA004480; -.
DR   MalaCards; AFG3L2; -.
DR   MIM; 604581; gene.
DR   MIM; 610246; phenotype.
DR   MIM; 614487; phenotype.
DR   neXtProt; NX_Q9Y4W6; -.
DR   OpenTargets; ENSG00000141385; -.
DR   Orphanet; 313772; Early-onset spastic ataxia-neuropathy syndrome.
DR   Orphanet; 101109; Spinocerebellar ataxia type 28.
DR   PharmGKB; PA24612; -.
DR   eggNOG; KOG0731; Eukaryota.
DR   eggNOG; COG0465; LUCA.
DR   GeneTree; ENSGT00870000136452; -.
DR   HOVERGEN; HBG050184; -.
DR   InParanoid; Q9Y4W6; -.
DR   KO; K08956; -.
DR   OMA; CLRLWGR; -.
DR   OrthoDB; EOG091G03EQ; -.
DR   PhylomeDB; Q9Y4W6; -.
DR   TreeFam; TF105004; -.
DR   BRENDA; 3.4.24.B18; 2681.
DR   GeneWiki; AFG3L2; -.
DR   GenomeRNAi; 10939; -.
DR   PRO; PR:Q9Y4W6; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; ENSG00000141385; -.
DR   CleanEx; HS_AFG3L2; -.
DR   ExpressionAtlas; Q9Y4W6; baseline and differential.
DR   Genevisible; Q9Y4W6; HS.
DR   GO; GO:0005745; C:m-AAA complex; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007409; P:axonogenesis; IMP:UniProtKB.
DR   GO; GO:0042407; P:cristae formation; IEA:Ensembl.
DR   GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0036444; P:mitochondrial calcium uptake; IMP:UniProtKB.
DR   GO; GO:0008053; P:mitochondrial fusion; IEA:Ensembl.
DR   GO; GO:0034982; P:mitochondrial protein processing; IEA:Ensembl.
DR   GO; GO:0048747; P:muscle fiber development; IEA:Ensembl.
DR   GO; GO:0042552; P:myelination; IEA:Ensembl.
DR   GO; GO:0021675; P:nerve development; IEA:Ensembl.
DR   GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0060013; P:righting reflex; IEA:Ensembl.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF06480; FtsH_ext; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Disease mutation;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion;
KW   Neurodegeneration; Nucleotide-binding; Protease; Reference proteome;
KW   Spinocerebellar ataxia; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN         1    797       AFG3-like protein 2.
FT                                /FTId=PRO_0000084673.
FT   TRANSMEM    143    163       Helical. {ECO:0000255}.
FT   TRANSMEM    251    271       Helical. {ECO:0000255}.
FT   NP_BIND     348    355       ATP. {ECO:0000255}.
FT   ACT_SITE    575    575       {ECO:0000250|UniProtKB:Q9WZ49}.
FT   METAL       574    574       Zinc; catalytic.
FT                                {ECO:0000250|UniProtKB:Q9WZ49}.
FT   METAL       578    578       Zinc; catalytic.
FT                                {ECO:0000250|UniProtKB:Q9WZ49}.
FT   METAL       649    649       Zinc; catalytic.
FT                                {ECO:0000250|UniProtKB:Q9WZ49}.
FT   MOD_RES     117    117       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8JZQ2}.
FT   VARIANT     432    432       N -> T (in SCA28; dbSNP:rs151344512).
FT                                {ECO:0000269|PubMed:20208537}.
FT                                /FTId=VAR_063544.
FT   VARIANT     616    616       Y -> C (in SPAX5; hypomorphic mutation;
FT                                results in impaired oligomerization with
FT                                itself and SPG7; retains ATPase and
FT                                proteolytic activities;
FT                                dbSNP:rs387906889).
FT                                {ECO:0000269|PubMed:22022284}.
FT                                /FTId=VAR_067330.
FT   VARIANT     654    654       T -> I (in SCA28; dbSNP:rs151344513).
FT                                {ECO:0000269|PubMed:20725928}.
FT                                /FTId=VAR_064402.
FT   VARIANT     666    666       M -> R (in SCA28; dbSNP:rs151344515).
FT                                {ECO:0000269|PubMed:20725928}.
FT                                /FTId=VAR_064403.
FT   VARIANT     666    666       M -> T (in SCA28; dbSNP:rs151344515).
FT                                {ECO:0000269|PubMed:20725928}.
FT                                /FTId=VAR_064404.
FT   VARIANT     666    666       M -> V (in SCA28; dbSNP:rs151344514).
FT                                {ECO:0000269|PubMed:20725928}.
FT                                /FTId=VAR_064405.
FT   VARIANT     671    671       G -> E (in SCA28; dbSNP:rs151344518).
FT                                {ECO:0000269|PubMed:20725928}.
FT                                /FTId=VAR_064406.
FT   VARIANT     671    671       G -> R (in SCA28; dbSNP:rs151344517).
FT                                {ECO:0000269|PubMed:20725928}.
FT                                /FTId=VAR_064407.
FT   VARIANT     689    689       Y -> H (in SCA28).
FT                                {ECO:0000269|PubMed:24293060}.
FT                                /FTId=VAR_075198.
FT   VARIANT     689    689       Y -> N (in SCA28).
FT                                {ECO:0000269|PubMed:26677414}.
FT                                /FTId=VAR_075199.
FT   VARIANT     691    691       E -> K (in SCA28; dbSNP:rs151344520).
FT                                {ECO:0000269|PubMed:20208537}.
FT                                /FTId=VAR_063545.
FT   VARIANT     694    694       A -> E (in SCA28; dbSNP:rs151344521).
FT                                {ECO:0000269|PubMed:20208537}.
FT                                /FTId=VAR_063546.
FT   VARIANT     700    700       E -> K (in SCA28; dbSNP:rs151344522).
FT                                {ECO:0000269|PubMed:20354562}.
FT                                /FTId=VAR_064408.
FT   VARIANT     702    702       R -> Q (in SCA28; dbSNP:rs151344523).
FT                                {ECO:0000269|PubMed:20208537}.
FT                                /FTId=VAR_063547.
FT   CONFLICT     74     74       E -> G (in Ref. 1; CAB48398).
FT                                {ECO:0000305}.
FT   CONFLICT    633    633       V -> A (in Ref. 1; CAB48398).
FT                                {ECO:0000305}.
FT   STRAND      165    169       {ECO:0000244|PDB:2LNA}.
FT   HELIX       172    178       {ECO:0000244|PDB:2LNA}.
FT   HELIX       180    182       {ECO:0000244|PDB:2LNA}.
FT   STRAND      185    191       {ECO:0000244|PDB:2LNA}.
FT   TURN        192    194       {ECO:0000244|PDB:2LNA}.
FT   STRAND      195    200       {ECO:0000244|PDB:2LNA}.
FT   TURN        202    204       {ECO:0000244|PDB:2LNA}.
FT   STRAND      212    215       {ECO:0000244|PDB:2LNA}.
FT   HELIX       219    232       {ECO:0000244|PDB:2LNA}.
FT   TURN        237    239       {ECO:0000244|PDB:2LNA}.
FT   STRAND      243    245       {ECO:0000244|PDB:2LNA}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       542    743       ipfam:Peptidase_M41 [T]
FT   MYHIT       150    240       ipfam:FtsH_ext [T]
FT   MYHIT         4    769       ihamap:FtsH [T]
FT   MYHIT       447    465       ipat:AAA [T]
FT   MYHIT       340    479       ismart:AAA [T]
FT   MYHIT       345    476       ipfam:AAA [T]
SQ   SEQUENCE   797 AA;  88584 MW;  EACBB7C5F2EE5E08 CRC64;
     MAHRCLRLWG RGGCWPRGLQ QLLVPGGVGP GEQPCLRTLY RFVTTQARAS RNSLLTDIIA
     AYQRFCSRPP KGFEKYFPNG KNGKKASEPK EVMGEKKESK PAATTRSSGG GGGGGGKRGG
     KKDDSHWWSR FQKGDIPWDD KDFRMFFLWT ALFWGGVMFY LLLKRSGREI TWKDFVNNYL
     SKGVVDRLEV VNKRFVRVTF TPGKTPVDGQ YVWFNIGSVD TFERNLETLQ QELGIEGENR
     VPVVYIAESD GSFLLSMLPT VLIIAFLLYT IRRGPAGIGR TGRGMGGLFS VGETTAKVLK
     DEIDVKFKDV AGCEEAKLEI MEFVNFLKNP KQYQDLGAKI PKGAILTGPP GTGKTLLAKA
     TAGEANVPFI TVSGSEFLEM FVGVGPARVR DLFALARKNA PCILFIDEID AVGRKRGRGN
     FGGQSEQENT LNQLLVEMDG FNTTTNVVIL AGTNRPDILD PALLRPGRFD RQIFIGPPDI
     KGRASIFKVH LRPLKLDSTL EKDKLARKLA SLTPGFSGAD VANVCNEAAL IAARHLSDSI
     NQKHFEQAIE RVIGGLEKKT QVLQPEEKKT VAYHEAGHAV AGWYLEHADP LLKVSIIPRG
     KGLGYAQYLP KEQYLYTKEQ LLDRMCMTLG GRVSEEIFFG RITTGAQDDL RKVTQSAYAQ
     IVQFGMNEKV GQISFDLPRQ GDMVLEKPYS EATARLIDDE VRILINDAYK RTVALLTEKK
     ADVEKVALLL LEKEVLDKND MVELLGPRPF AEKSTYEEFV EGTGSLDEDT SLPEGLKDWN
     KEREKEKEEP PGEKVAN
//