ACV1C_HUMAN
ID ACV1C_HUMAN Reviewed; 493 AA.
AC Q8NER5; Q4ZFZ8; Q86UL1; Q86UL2; Q8TBG2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Activin receptor type-1C;
DE EC=2.7.11.30;
DE AltName: Full=Activin receptor type IC;
DE Short=ACTR-IC;
DE AltName: Full=Activin receptor-like kinase 7;
DE Short=ALK-7;
DE Flags: Precursor;
GN Name=ACVR1C {ECO:0000312|HGNC:HGNC:18123};
GN Synonyms=ALK7 {ECO:0000303|PubMed:12606401};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF LYS-222.
RC TISSUE=Brain {ECO:0000269|PubMed:12063393};
RX PubMed=12063393; DOI=10.1159/000059339;
RA Bondestam J., Huotari M.-A., Moren A., Ustinov J., Kaivo-Oja N., Kallio J.,
RA Horelli-Kuitunen N., Aaltonen J., Fujii M., Moustakas A., Ten Dijke P.,
RA Otonkoski T., Ritvos O.;
RT "cDNA cloning, expression studies and chromosome mapping of human type I
RT serine/threonine kinase receptor ALK7 (ACVR1C).";
RL Cytogenet. Cell Genet. 95:157-162(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAP21994.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Placenta {ECO:0000312|EMBL:AAM93495.1};
RX PubMed=12606401; DOI=10.1095/biolreprod.102.013045;
RA Roberts H.J., Hu S., Qiu Q., Leung P.C.K., Caniggia I., Gruslin A.,
RA Tsang B., Peng C.;
RT "Identification of novel isoforms of activin receptor-like kinase 7 (ALK7)
RT generated by alternative splicing and expression of ALK7 and its ligand,
RT Nodal, in human placenta.";
RL Biol. Reprod. 68:1719-1726(2003).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAX88951.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH22530.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH22530.1};
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF THR-194 AND LYS-222.
RX PubMed=15531507; DOI=10.1210/jc.2004-0893;
RA Xu G., Zhong Y., Munir S., Yang B.B., Tsang B.K., Peng C.;
RT "Nodal induces apoptosis and inhibits proliferation in human epithelial
RT ovarian cancer cells via activin receptor-like kinase 7.";
RL J. Clin. Endocrinol. Metab. 89:5523-5534(2004).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-195; ARG-216; ARG-267; VAL-355 AND
RP VAL-482.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Serine/threonine protein kinase which forms a receptor
CC complex on ligand binding. The receptor complex consisting of 2 type II
CC and 2 type I transmembrane serine/threonine kinases. Type II receptors
CC phosphorylate and activate type I receptors which autophosphorylate,
CC then bind and activate SMAD transcriptional regulators, SMAD2 and
CC SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in
CC cell differentiation, growth arrest and apoptosis.
CC {ECO:0000269|PubMed:12063393, ECO:0000269|PubMed:15531507}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC -!- SUBUNIT: Binds the type 2 receptor protein ACVR2A. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12606401}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:12606401}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:12606401};
CC IsoId=Q8NER5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12606401}; Synonyms=B
CC {ECO:0000303|PubMed:12606401}, soluble B {ECO:0000303|PubMed:12606401};
CC IsoId=Q8NER5-2; Sequence=VSP_051841;
CC Name=3 {ECO:0000269|PubMed:12606401}; Synonyms=A
CC {ECO:0000303|PubMed:12606401}, soluble A {ECO:0000303|PubMed:12606401};
CC IsoId=Q8NER5-3; Sequence=VSP_051842;
CC Name=4 {ECO:0000269|PubMed:12606401}; Synonyms=Truncated
CC {ECO:0000303|PubMed:12606401};
CC IsoId=Q8NER5-4; Sequence=VSP_051840;
CC -!- TISSUE SPECIFICITY: Present in pancreas, heart, colon, small intestine,
CC ovary and the hippocampus, medulla oblongata and putamen of the brain.
CC Isoform 1, isoform 2, isoform 3 and isoform 4 are all expressed in the
CC placenta throughout pregnancy. {ECO:0000269|PubMed:12063393,
CC ECO:0000269|PubMed:12606401}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; AY127050; AAM93495.1; -; mRNA.
DR EMBL; AF525679; AAP21993.1; -; mRNA.
DR EMBL; AF525680; AAP21994.1; -; mRNA.
DR EMBL; AF525681; AAP21995.1; -; mRNA.
DR EMBL; AC019186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079750; AAX88951.1; -; Genomic_DNA.
DR EMBL; BC022530; AAH22530.1; -; mRNA.
DR CCDS; CCDS2205.1; -. [Q8NER5-1]
DR CCDS; CCDS46432.1; -. [Q8NER5-2]
DR CCDS; CCDS46433.1; -. [Q8NER5-3]
DR CCDS; CCDS46434.1; -. [Q8NER5-4]
DR RefSeq; NP_001104501.1; NM_001111031.1. [Q8NER5-4]
DR RefSeq; NP_001104502.1; NM_001111032.1. [Q8NER5-3]
DR RefSeq; NP_001104503.1; NM_001111033.1. [Q8NER5-2]
DR RefSeq; NP_660302.2; NM_145259.2. [Q8NER5-1]
DR AlphaFoldDB; Q8NER5; -.
DR SMR; Q8NER5; -.
DR BioGRID; 126232; 21.
DR IntAct; Q8NER5; 3.
DR STRING; 9606.ENSP00000243349; -.
DR ChEMBL; CHEMBL5642; -.
DR iPTMnet; Q8NER5; -.
DR PhosphoSitePlus; Q8NER5; -.
DR BioMuta; ACVR1C; -.
DR DMDM; 74762565; -.
DR jPOST; Q8NER5; -.
DR MassIVE; Q8NER5; -.
DR MaxQB; Q8NER5; -.
DR PaxDb; Q8NER5; -.
DR PeptideAtlas; Q8NER5; -.
DR PRIDE; Q8NER5; -.
DR ProteomicsDB; 73204; -. [Q8NER5-1]
DR ProteomicsDB; 73205; -. [Q8NER5-2]
DR ProteomicsDB; 73206; -. [Q8NER5-3]
DR ProteomicsDB; 73207; -. [Q8NER5-4]
DR Antibodypedia; 2075; 422 antibodies from 35 providers.
DR DNASU; 130399; -.
DR Ensembl; ENST00000243349.13; ENSP00000243349.7; ENSG00000123612.16. [Q8NER5-1]
DR Ensembl; ENST00000335450.7; ENSP00000335178.7; ENSG00000123612.16. [Q8NER5-3]
DR Ensembl; ENST00000348328.9; ENSP00000335139.6; ENSG00000123612.16. [Q8NER5-2]
DR Ensembl; ENST00000409680.7; ENSP00000387168.3; ENSG00000123612.16. [Q8NER5-4]
DR GeneID; 130399; -.
DR KEGG; hsa:130399; -.
DR MANE-Select; ENST00000243349.13; ENSP00000243349.7; NM_145259.3; NP_660302.2.
DR UCSC; uc002tzk.5; human. [Q8NER5-1]
DR CTD; 130399; -.
DR DisGeNET; 130399; -.
DR GeneCards; ACVR1C; -.
DR HGNC; HGNC:18123; ACVR1C.
DR HPA; ENSG00000123612; Tissue enriched (adipose).
DR MIM; 608981; gene.
DR neXtProt; NX_Q8NER5; -.
DR OpenTargets; ENSG00000123612; -.
DR PharmGKB; PA134908988; -.
DR VEuPathDB; HostDB:ENSG00000123612; -.
DR eggNOG; KOG2052; Eukaryota.
DR GeneTree; ENSGT00940000158842; -.
DR HOGENOM; CLU_000288_8_1_1; -.
DR InParanoid; Q8NER5; -.
DR OMA; ICTCQGR; -.
DR OrthoDB; 776697at2759; -.
DR PhylomeDB; Q8NER5; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.11.30; 2681.
DR PathwayCommons; Q8NER5; -.
DR Reactome; R-HSA-1181150; Signaling by NODAL.
DR Reactome; R-HSA-1433617; Regulation of signaling by NODAL.
DR Reactome; R-HSA-1502540; Signaling by Activin.
DR SignaLink; Q8NER5; -.
DR SIGNOR; Q8NER5; -.
DR BioGRID-ORCS; 130399; 7 hits in 1107 CRISPR screens.
DR ChiTaRS; ACVR1C; human.
DR GeneWiki; ACVR1C; -.
DR GenomeRNAi; 130399; -.
DR Pharos; Q8NER5; Tbio.
DR PRO; PR:Q8NER5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NER5; protein.
DR Bgee; ENSG00000123612; Expressed in jejunal mucosa and 129 other tissues.
DR Genevisible; Q8NER5; HS.
DR GO; GO:0048179; C:activin receptor complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0016361; F:activin receptor activity, type I; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019838; F:growth factor binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IC:UniProtKB.
DR GO; GO:0038100; F:nodal binding; IMP:BHF-UCL.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0032924; P:activin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030262; P:apoptotic nuclear changes; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR GO; GO:1901383; P:negative regulation of chorionic trophoblast cell proliferation; IMP:BHF-UCL.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:1901164; P:negative regulation of trophoblast cell migration; IDA:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0038092; P:nodal signaling pathway; IMP:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0001834; P:trophectodermal cell proliferation; IDA:MGI.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR003605; GS_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08515; TGF_beta_GS; 1.
DR SMART; SM00467; GS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS51256; GS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; ATP-binding; Kinase; Magnesium; Manganese;
KW Membrane; Metal-binding; Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..493
FT /note="Activin receptor type-1C"
FT /id="PRO_0000042628"
FT TOPO_DOM 22..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 165..194
FT /note="GS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT DOMAIN 195..485
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 323
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q04771,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 201..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q04771,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q04771,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12606401"
FT /id="VSP_051840"
FT VAR_SEQ 102..258
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12606401"
FT /id="VSP_051841"
FT VAR_SEQ 102..181
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12606401"
FT /id="VSP_051842"
FT VARIANT 195
FT /note="I -> T (in dbSNP:rs56188432)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041407"
FT VARIANT 216
FT /note="G -> R (in dbSNP:rs34742924)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041408"
FT VARIANT 267
FT /note="W -> R (in a lung squamous cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041409"
FT VARIANT 355
FT /note="I -> V (in dbSNP:rs35500979)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041410"
FT VARIANT 482
FT /note="I -> V (in dbSNP:rs7594480)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041411"
FT MUTAGEN 194
FT /note="T->D: Pro-apoptotic."
FT /evidence="ECO:0000269|PubMed:15531507"
FT MUTAGEN 222
FT /note="K->R: Loss of response to NODAL and SMAD2
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:12063393,
FT ECO:0000269|PubMed:15531507"
FT CONFLICT 231
FT /note="S -> Y (in Ref. 4; AAH22530)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="V -> M (in Ref. 4; AAH22530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 54871 MW; 5A10F259679204CB CRC64;
MTRALCSALR QALLLLAAAA ELSPGLKCVC LLCDSSNFTC QTEGACWASV MLTNGKEQVI
KSCVSLPELN AQVFCHSSNN VTKTECCFTD FCNNITLHLP TASPNAPKLG PMELAIIITV
PVCLLSIAAM LTVWACQGRQ CSYRKKKRPN VEEPLSECNL VNAGKTLKDL IYDVTASGSG
SGLPLLVQRT IARTIVLQEI VGKGRFGEVW HGRWCGEDVA VKIFSSRDER SWFREAEIYQ
TVMLRHENIL GFIAADNKDN GTWTQLWLVS EYHEQGSLYD YLNRNIVTVA GMIKLALSIA
SGLAHLHMEI VGTQGKPAIA HRDIKSKNIL VKKCETCAIA DLGLAVKHDS ILNTIDIPQN
PKVGTKRYMA PEMLDDTMNV NIFESFKRAD IYSVGLVYWE IARRCSVGGI VEEYQLPYYD
MVPSDPSIEE MRKVVCDQKF RPSIPNQWQS CEALRVMGRI MRECWYANGA ARLTALRIKK
TISQLCVKED CKA
