Entry sw:ZN532_HUMAN

ID   ZN532_HUMAN             Reviewed;        1301 AA.
AC   Q9HCE3; Q4G0V6; Q7L7Z7; Q96QR7; Q9NVJ6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   30-NOV-2016, entry version 113.
DE   RecName: Full=Zinc finger protein 532;
GN   Name=ZNF532; Synonyms=KIAA1629;
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].
RA   Chen H., Wang N., DePaulo R.J. Jr., Ross C.A., McInnis M.G.;
RT   "Identification of the full-length cDNA for a novel zinc finger gene
RT   on human chromosome 18q21 as a candidate for bipolar disorder.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes.
RT   XVIII. The complete sequences of 100 new cDNA clones from brain which
RT   code for large proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 681-1301.
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-133; SER-134;
RP   SER-252; SER-307; SER-314; SER-434 AND SER-1140, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-1140, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] LEU-822.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 12 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH36366.1; Type=Frameshift; Positions=1077; Evidence={ECO:0000305};
CC       Sequence=BAA91755.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB13455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AY039256; AAK72122.1; -; mRNA.
DR   EMBL; AB046849; BAB13455.1; ALT_INIT; mRNA.
DR   EMBL; BC036366; AAH36366.1; ALT_FRAME; mRNA.
DR   EMBL; BC130618; AAI30619.1; -; mRNA.
DR   EMBL; BC130620; AAI30621.1; -; mRNA.
DR   EMBL; AK001559; BAA91755.1; ALT_INIT; mRNA.
DR   CCDS; CCDS11969.1; -.
DR   RefSeq; NP_001305655.1; NM_001318726.1.
DR   RefSeq; NP_001305656.1; NM_001318727.1.
DR   RefSeq; NP_001305657.1; NM_001318728.1.
DR   RefSeq; NP_060651.2; NM_018181.5.
DR   RefSeq; XP_016881301.1; XM_017025812.1.
DR   RefSeq; XP_016881302.1; XM_017025813.1.
DR   RefSeq; XP_016881303.1; XM_017025814.1.
DR   RefSeq; XP_016881304.1; XM_017025815.1.
DR   RefSeq; XP_016881305.1; XM_017025816.1.
DR   RefSeq; XP_016881306.1; XM_017025817.1.
DR   RefSeq; XP_016881307.1; XM_017025818.1.
DR   UniGene; Hs.529023; -.
DR   UniGene; Hs.607676; -.
DR   ProteinModelPortal; Q9HCE3; -.
DR   SMR; Q9HCE3; -.
DR   BioGrid; 120501; 3.
DR   IntAct; Q9HCE3; 3.
DR   STRING; 9606.ENSP00000338217; -.
DR   iPTMnet; Q9HCE3; -.
DR   PhosphoSitePlus; Q9HCE3; -.
DR   BioMuta; ZNF532; -.
DR   DMDM; 158564020; -.
DR   EPD; Q9HCE3; -.
DR   MaxQB; Q9HCE3; -.
DR   PaxDb; Q9HCE3; -.
DR   PeptideAtlas; Q9HCE3; -.
DR   PRIDE; Q9HCE3; -.
DR   Ensembl; ENST00000336078; ENSP00000338217; ENSG00000074657.
DR   Ensembl; ENST00000589288; ENSP00000466007; ENSG00000074657.
DR   Ensembl; ENST00000591083; ENSP00000468532; ENSG00000074657.
DR   Ensembl; ENST00000591230; ENSP00000465709; ENSG00000074657.
DR   Ensembl; ENST00000591808; ENSP00000468238; ENSG00000074657.
DR   GeneID; 55205; -.
DR   KEGG; hsa:55205; -.
DR   UCSC; uc002lho.4; human.
DR   CTD; 55205; -.
DR   DisGeNET; 55205; -.
DR   GeneCards; ZNF532; -.
DR   HGNC; HGNC:30940; ZNF532.
DR   HPA; HPA015322; -.
DR   neXtProt; NX_Q9HCE3; -.
DR   OpenTargets; ENSG00000074657; -.
DR   PharmGKB; PA134901858; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00530000063261; -.
DR   HOGENOM; HOG000010306; -.
DR   HOVERGEN; HBG062228; -.
DR   InParanoid; Q9HCE3; -.
DR   OMA; FQSHVTK; -.
DR   OrthoDB; EOG091G0AA1; -.
DR   PhylomeDB; Q9HCE3; -.
DR   TreeFam; TF329009; -.
DR   BioCyc; ZFISH:ENSG00000074657-MONOMER; -.
DR   ChiTaRS; ZNF532; human.
DR   GenomeRNAi; 55205; -.
DR   PRO; PR:Q9HCE3; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; ENSG00000074657; -.
DR   CleanEx; HS_ZNF532; -.
DR   ExpressionAtlas; Q9HCE3; baseline and differential.
DR   Genevisible; Q9HCE3; HS.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 2.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF16622; zf-C2H2_11; 1.
DR   Pfam; PF13912; zf-C2H2_6; 1.
DR   SMART; SM00355; ZnF_C2H2; 15.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1301       Zinc finger protein 532.
FT                                /FTId=PRO_0000299552.
FT   ZN_FING     616    635       C2H2-type 1; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     754    779       C2H2-type 2; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     783    805       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     842    865       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     870    893       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     905    927       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     936    959       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1025   1048       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1055   1078       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1085   1111       C2H2-type 10; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING    1203   1226       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1264   1286       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   MOD_RES     130    130       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     133    133       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     134    134       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     175    175       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q6NXK2}.
FT   MOD_RES     205    205       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     252    252       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     307    307       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     314    314       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     434    434       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES    1140   1140       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   VARIANT     761    761       E -> D (in dbSNP:rs3737506).
FT                                /FTId=VAR_034846.
FT   VARIANT     822    822       S -> L (in a breast cancer sample;
FT                                somatic mutation; dbSNP:rs771503724).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035585.
FT   CONFLICT    972    972       G -> S (in Ref. 3; AAH36366).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT      1055   1078       ismart:ZnF_C2H2 [T]
FT   MYHIT       905    927       ismart:ZnF_C2H2 [T]
FT   MYHIT       936    964       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       844    865       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       783    805       ismart:ZnF_C2H2 [T]
FT   MYHIT       785    807       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT      1264   1286       ismart:ZnF_C2H2 [T]
FT   MYHIT      1055   1083       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       907    927       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       754    784       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       811    835       ismart:ZnF_C2H2 [T]
FT   MYHIT       936    959       ismart:ZnF_C2H2 [T]
FT   MYHIT       842    865       ismart:ZnF_C2H2 [T]
FT   MYHIT       616    634       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       870    893       ismart:ZnF_C2H2 [T]
FT   MYHIT      1205   1226       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT      1264   1286       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       872    893       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       644    668       ismart:ZnF_C2H2 [T]
FT   MYHIT      1266   1286       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT      1025   1048       ismart:ZnF_C2H2 [T]
FT   MYHIT      1085   1111       ismart:ZnF_C2H2 [T]
FT   MYHIT      1057   1078       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT      1203   1231       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT      1203   1226       ismart:ZnF_C2H2 [T]
FT   MYHIT      1174   1196       ismart:ZnF_C2H2 [T]
FT   MYHIT       870    898       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       905    932       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       754    774       ismart:ZnF_C2H2 [T]
FT   MYHIT       938    959       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       616    636       ismart:ZnF_C2H2 [T]
SQ   SEQUENCE   1301 AA;  141696 MW;  434E9519D144904A CRC64;
     MTMGDMKTPD FDDLLAAFDI PDMVDPKAAI ESGHDDHESH MKQNAHGEDD SHAPSSSDVG
     VSVIVKNVRN IDSSEGGEKD GHNPTGNGLH NGFLTASSLD SYSKDGAKSL KGDVPASEVT
     LKDSTFSQFS PISSAEEFDD DEKIEVDDPP DKEDMRSSFR SNVLTGSAPQ QDYDKLKALG
     GENSSKTGLS TSGNVEKNKA VKRETEASSI NLSVYEPFKV RKAEDKLKES SDKVLENRVL
     DGKLSSEKND TSLPSVAPSK TKSSSKLSSC IAAIAALSAK KAASDSCKEP VANSRESSPL
     PKEVNDSPRA ADKSPESQNL IDGTKKPSLK QPDSPRSISS ENSSKGSPSS PAGSTPAIPK
     VRIKTIKTSS GEIKRTVTRV LPEVDLDSGK KPSEQTASVM ASVTSLLSSP ASAAVLSSPP
     RAPLQSAVVT NAVSPAELTP KQVTIKPVAT AFLPVSAVKT AGSQVINLKL ANNTTVKATV
     ISAASVQSAS SAIIKAANAI QQQTVVVPAS SLANAKLVPK TVHLANLNLL PQGAQATSEL
     RQVLTKPQQQ IKQAIINAAA SQPPKKVSRV QVVSSLQSSV VEAFNKVLSS VNPVPVYIPN
     LSPPANAGIT LPTRGYKCLE CGDSFALEKS LTQHYDRRSV RIEVTCNHCT KNLVFYNKCS
     LLSHARGHKE KGVVMQCSHL ILKPVPADQM IVSPSSNTST STSTLQSPVG AGTHTVTKIQ
     SGITGTVISA PSSTPITPAM PLDEDPSKLC RHSLKCLECN EVFQDETSLA THFQQAADTS
     GQKTCTICQM LLPNQCSYAS HQRIHQHKSP YTCPECGAIC RSVHFQTHVT KNCLHYTRRV
     GFRCVHCNVV YSDVAALKSH IQGSHCEVFY KCPICPMAFK SAPSTHSHAY TQHPGIKIGE
     PKIIYKCSMC DTVFTLQTLL YRHFDQHIEN QKVSVFKCPD CSLLYAQKQL MMDHIKSMHG
     TLKSIEGPPN LGINLPLSIK PATQNSANQN KEDTKSMNGK EKLEKKSPSP VKKSMETKKV
     ASPGWTCWEC DCLFMQRDVY ISHVRKEHGK QMKKHPCRQC DKSFSSSHSL CRHNRIKHKG
     IRKVYACSHC PDSRRTFTKR LMLEKHVQLM HGIKDPDLKE MTDATNEEET EIKEDTKVPS
     PKRKLEEPVL EFRPPRGAIT QPLKKLKINV FKVHKCAVCG FTTENLLQFH EHIPQHKSDG
     SSYQCRECGL CYTSHVSLSR HLFIVHKLKE PQPVSKQNGA GEDNQQENKP SHEDESPDGA
     VSDRKCKVCA KTFETEAALN THMRTHGMAF IKSKRMSSAE K
//