ID WASC2_MOUSE Reviewed; 1334 AA.
AC Q6PGL7; Q3TQ99; Q80TW8; Q80UQ4; Q8CAP0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 10-MAY-2017, entry version 85.
DE RecName: Full=WASH complex subunit 2 {ECO:0000312|MGI:MGI:106463};
GN Name=Washc2 {ECO:0000312|MGI:MGI:106463};
GN Synonyms=D6Wsu116e, Fam21, Kiaa0592;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT cDNAs identified by screening of terminal sequences of cDNA clones
RT randomly sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in
RT naive and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-284;
RP SER-388; SER-533; SER-613; SER-614; SER-723; SER-747; SER-1169;
RP SER-1172; SER-1173 AND SER-1333, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614 AND SER-747, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of
RT electron capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-322; SER-533;
RP SER-613; SER-614; SER-723; SER-747; SER-752; SER-798; SER-870;
RP SER-873; SER-1169 AND SER-1172, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and
RT expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts at least in part as component of the WASH core
CC complex whose assembly at the surface of endosomes inhibits WASH
CC nucleation-promoting factor (NPF) activity in recruiting and
CC activating the Arp2/3 complex to induce actin polymerization and
CC is involved in the fission of tubules that serve as transport
CC intermediates during endosome sorting. Mediates the recruitment of
CC the WASH core complex to endosome membranes via binding to
CC phospholipids and VPS35 of the retromer CSC. Mediates the
CC recruitment of the F-actin-capping protein dimer to the WASH core
CC complex probably promoting localized F-actin polymerization needed
CC for vesicle scission. Via its C-terminus binds various
CC phospholipids, most strongly phosphatidylinositol 4-phosphate
CC (PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and
CC phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved
CC in the endosome-to-plasma membrane trafficking and recycling of
CC SNX27-retromer-dependent cargo proteins, such as GLUT1. Required
CC for the association of DNAJC13, SDCCAG3, ANKRD50 with retromer CSC
CC subunit VPS35. Required for the endosomal recruitment of CCC
CC complex subunits COMMD1, CCDC93 and C16orf62 homolog (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC regulatory complex SHRC composed of WASHC1, WASHC2, WASHC3, WASHC4
CC and WASHC5; in the complex interacts (via N-terminus) directly
CC with WASHC1. The WASH core complex associates with the F-actin-
CC capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and
CC CAPZB) in a transient or substoichiometric manner which was
CC initially described as WASH complex. Interacts with VPS35;
CC mediates the association with the retromer CSC complex. Interacts
CC with FKBP15. Interacts with CCDC93, CCDC22, C16orf62 homolog;
CC indicative for an association of the WASH core complex with the
CC CCC complex (By similarity). {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9Y4E1}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PGL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGL7-2; Sequence=VSP_030949;
CC Note=No experimental confirmation available.;
CC -!- DOMAIN: The LFa (leucine-phenylalanine-acidic) motif bind directly
CC to VPS35 of retromer CSC; adjacent motifs can act cooperatively to
CC bind multiple CSCs, although there is significant variability in
CC the affinities of different motifs for retromer.
CC {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- SIMILARITY: Belongs to the FAM21 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49979.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK122320; BAC65602.2; -; Transcribed_RNA.
DR EMBL; AK163765; BAE37485.1; -; mRNA.
DR EMBL; AK038318; BAC29966.1; -; mRNA.
DR EMBL; BC049979; AAH49979.1; ALT_SEQ; mRNA.
DR EMBL; BC056942; AAH56942.1; -; mRNA.
DR CCDS; CCDS20450.1; -. [Q6PGL7-1]
DR RefSeq; NP_080861.2; NM_026585.3. [Q6PGL7-1]
DR UniGene; Mm.28524; -.
DR ProteinModelPortal; Q6PGL7; -.
DR SMR; Q6PGL7; -.
DR IntAct; Q6PGL7; 3.
DR MINT; MINT-1864605; -.
DR STRING; 10090.ENSMUSP00000038983; -.
DR iPTMnet; Q6PGL7; -.
DR PhosphoSitePlus; Q6PGL7; -.
DR EPD; Q6PGL7; -.
DR PaxDb; Q6PGL7; -.
DR PeptideAtlas; Q6PGL7; -.
DR PRIDE; Q6PGL7; -.
DR Ensembl; ENSMUST00000036759; ENSMUSP00000038983; ENSMUSG00000024104. [Q6PGL7-1]
DR GeneID; 28006; -.
DR KEGG; mmu:28006; -.
DR UCSC; uc009djs.2; mouse. [Q6PGL7-1]
DR CTD; 28006; -.
DR MGI; MGI:106463; Washc2.
DR eggNOG; ENOG410IEJH; Eukaryota.
DR eggNOG; ENOG4110AMY; LUCA.
DR GeneTree; ENSGT00510000047694; -.
DR HOGENOM; HOG000112469; -.
DR HOVERGEN; HBG055529; -.
DR InParanoid; Q6PGL7; -.
DR KO; K18462; -.
DR OMA; HSDNDQN; -.
DR OrthoDB; EOG091G05P8; -.
DR PhylomeDB; Q6PGL7; -.
DR TreeFam; TF329309; -.
DR PRO; PR:Q6PGL7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000024104; -.
DR ExpressionAtlas; Q6PGL7; baseline and differential.
DR Genevisible; Q6PGL7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:MGI.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISO:MGI.
DR GO; GO:1905394; F:retromer complex binding; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR InterPro; IPR027308; FAM21.
DR InterPro; IPR029341; FAM21/CAPZIP.
DR PANTHER; PTHR21669:SF21; PTHR21669:SF21; 1.
DR Pfam; PF15255; CAP-ZIP_m; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Endosome;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 1334 WASH complex subunit 2.
FT /FTId=PRO_0000317433.
FT REGION 1 219 Sufficient for interaction with WASHC3,
FT WASHC4 and WASHC5; required for
FT interaction with WASHC1.
FT {ECO:0000250|UniProtKB:Q9Y4E1}.
FT REGION 347 594 Sufficient for interaction with CCDC93.
FT {ECO:0000250|UniProtKB:Q9Y4E1}.
FT REGION 348 1334 Interaction with VPS35.
FT {ECO:0000250|UniProtKB:Q9Y4E1}.
FT REGION 932 1334 Interaction with phospholipids.
FT {ECO:0000250|UniProtKB:Q9Y4E1}.
FT REGION 1024 1042 Required for interaction with F-actin-
FT capping protein subunit alpha (CAPZA1 or
FT CAPZA2 or CAPZA3).
FT {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 358 368 LFa 1. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 441 457 LFa 2. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 476 485 LFa 3. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 531 542 LFa 4. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 566 577 LFa 5. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 658 670 LFa 6. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 686 698 LFa 7. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 835 843 LFa 8. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 852 858 LFa 9. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 874 884 LFa 10. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 1124 1131 LFa 11. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 1164 1178 LFa 12. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 1194 1202 LFa 13. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 1227 1233 LFa 14. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 1255 1263 LFa 15. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 1283 1292 LFa 16. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT MOTIF 1323 1331 LFa 17. {ECO:0000250|UniProtKB:Q9Y4E1}.
FT COMPBIAS 221 228 Poly-Glu.
FT COMPBIAS 443 453 Poly-Asp.
FT COMPBIAS 661 665 Poly-Asp.
FT COMPBIAS 780 783 Poly-Ser.
FT MOD_RES 157 157 Phosphoserine.
FT {ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 159 159 Phosphoserine.
FT {ECO:0000244|PubMed:19144319}.
FT MOD_RES 204 204 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q80X08}.
FT MOD_RES 205 205 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q80X08}.
FT MOD_RES 209 209 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q80X08}.
FT MOD_RES 284 284 Phosphoserine.
FT {ECO:0000244|PubMed:19144319}.
FT MOD_RES 322 322 Phosphothreonine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 388 388 Phosphoserine.
FT {ECO:0000244|PubMed:19144319}.
FT MOD_RES 533 533 Phosphoserine.
FT {ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 538 538 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q80X08}.
FT MOD_RES 613 613 Phosphoserine.
FT {ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 614 614 Phosphoserine.
FT {ECO:0000244|PubMed:19131326,
FT ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 723 723 Phosphoserine.
FT {ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 747 747 Phosphoserine.
FT {ECO:0000244|PubMed:17242355,
FT ECO:0000244|PubMed:19131326,
FT ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 752 752 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 783 783 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q80X08}.
FT MOD_RES 798 798 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 870 870 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 873 873 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 1049 1049 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q641Q2}.
FT MOD_RES 1067 1067 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q80X08}.
FT MOD_RES 1084 1084 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q641Q2}.
FT MOD_RES 1109 1109 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q641Q2}.
FT MOD_RES 1169 1169 Phosphoserine.
FT {ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 1172 1172 Phosphoserine.
FT {ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 1173 1173 Phosphoserine.
FT {ECO:0000244|PubMed:19144319}.
FT MOD_RES 1333 1333 Phosphoserine.
FT {ECO:0000244|PubMed:19144319}.
FT VAR_SEQ 866 952 SSVPSGGSLFGDDEDDDLFSSAKTQPVVPEKKGTLKKDHPV
FT SLKNQDPLDSTQGSKEKSTWKTEPAQDSSGLTPFKSREPSS
FT RIGKI -> V (in isoform 2).
FT {ECO:0000303|PubMed:12693553}.
FT /FTId=VSP_030949.
FT CONFLICT 385 385 L -> S (in Ref. 3; AAH49979).
FT {ECO:0000305}.
FT CONFLICT 556 556 P -> S (in Ref. 3; AAH49979).
FT {ECO:0000305}.
FT CONFLICT 630 630 A -> V (in Ref. 1; BAC65602).
FT {ECO:0000305}.
FT CONFLICT 910 910 N -> S (in Ref. 2; BAC29966).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 939 1072 ipfam:CAP-ZIP_m [T]
SQ SEQUENCE 1334 AA; 145311 MW; AD35C3FFAC27C159 CRC64;
MNRTSPDSER PPASEPVWER PWSVEEIRRS SQNWSLAADA GLLQFLQEFS QQTISRTHEI
KKQVDGLIQE TKATHCRLHN VFNDFLMLSN TQFIENRVYD EEVEEQVLKA EAEKAEQEKT
REQKEIDLIP KVQEAVNYGL QVLDSAFEQL DIKAGNSDSE EDDANERVDL ILEPKDLYID
RPLPYLIGSK LFMEQEDVGL GELSSEEGSV GSDRGSIVDS EDEKEEEESD EDFASHSDND
QNQHTTQISD EEEDDDGDLF ADSEKEGDDI EDIEESAKSK RPTSFADELA ARIKGDISNQ
RKEGQTDGKP QKTVKEKKER RTPADDEEDI LFPPPTLTDE DFSPFGSRGG LFSNGQGLFD
DEDESDLFKE APRARPAQAP VSEELPPSPK PGKKIPAGAV SVLLGHPDVS GSTSAPSLKE
LQKHGQPTPG KSSHLPTPAG LFDDDDNDND EDDNNFFMPS SSKPSKTDKV KSTAIIFDDD
EGDLFKEKAE ALPAASVSQT HESKTRADKT IALPSSKNLK LVSETKTQKG LFSDEEDSED
LFSSQSSSKP KSASLPSSQP PTSVSLFGDE DEEDSLFGSA AAKKQTSSLQ PQSQEKAKPS
EQPSKKTSAL LFSSDEEDQW NIADSHTKLA SDNKSKGELW DSGATQGQEA KAVKKTNLFE
DDDDDEVDLF AIAKDSQKKT QRTSLLFEDD AESGSSLFGL PPTSVPSATT KKESVPKVPL
LFSDEEDSEV PSGVKPEDLK VDNARVSPEV GSADVASIAQ KEGLLPASDQ EAGGPSDIFS
SSSPLDKGAK GRTRTVLSLF DEDEDKVEDE SSTCAPQDGR EKGLKTDSRP KSTGVFQDEE
LLFSHKLQKD NDPDVDLFAG TKKIRSSVPS GGSLFGDDED DDLFSSAKTQ PVVPEKKGTL
KKDHPVSLKN QDPLDSTQGS KEKSTWKTEP AQDSSGLTPF KSREPSSRIG KIQANLAINP
AALLPTVALQ IPGTKPVSSE LAFPSSEPGR SHILESVPTL PGSVEAGVSF DLPAQADTLH
SANKSRVKVR GKRRPQTRAA RRLAAQESSE AEDVTVDRGP VAQLSSSPVL PNGHQPLLQP
RMASGQTSSE TATAPPWEGG PVLSAADRSF FVKSRPQTGN EADLFDSGDI FPKSRGSQSV
EGAGVMAGEP PSHSSGGRKE KSLAFPDLSE GSSTEDLFQS VKPRAAKNRN PFPLLEDEED
LFADPRGKKN ERKPDSHQDS VSKTHDIFED DIFATEAIKP FPKKREKGRT LEPNLFDDNI
DIFADLTVKP KEKSKKKVAA KSMFDDDTDD IFSSGLQAKA SKPKSQSAEA ASEQRSEHKV
ASIFDDPLNA FGSQ
//
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