CO8A1_HUMAN
ID CO8A1_HUMAN Reviewed; 744 AA.
AC P27658; D3DN42; Q53XI6; Q96D07;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Collagen alpha-1(VIII) chain;
DE AltName: Full=Endothelial collagen;
DE Contains:
DE RecName: Full=Vastatin;
DE Flags: Precursor;
GN Name=COL8A1; Synonyms=C3orf7;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2029894; DOI=10.1111/j.1432-1033.1991.tb15951.x;
RA Muragaki Y., Mattei M.-G., Yamaguchi N., Olsen B.R., Ninomiya Y.;
RT "The complete primary structure of the human alpha 1 (VIII) chain and
RT assignment of its gene (COL8A1) to chromosome 3.";
RL Eur. J. Biochem. 197:615-622(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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]
RP TISSUE SPECIFICITY.
RX PubMed=2376131; DOI=10.3109/03008209009152157;
RA Kittelberger R., Davis P.F., Flynn D.W., Greenhill N.S.;
RT "Distribution of type VIII collagen in tissues: an immunohistochemical
RT study.";
RL Connect. Tissue Res. 24:303-318(1990).
RN [6]
RP PROTEOLYTIC PROCESSING.
RX PubMed=1515454; DOI=10.1016/0925-4439(92)90103-t;
RA Kittelberger R., Neale T.J., Francky K.T., Greenhill N.S., Gibson G.J.;
RT "Cleavage of type VIII collagen by human neutrophil elastase.";
RL Biochim. Biophys. Acta 1139:295-299(1992).
RN [7]
RP TISSUE SPECIFICITY, AND POSSIBLE FUNCTION.
RX PubMed=7734329;
RA Ruger B., Dunbar P.R., Hasan Q., Sawada H., Kittelberger R., Greenhill N.,
RA Neale T.J.;
RT "Human mast cells produce type VIII collagen in vivo.";
RL Int. J. Exp. Pathol. 75:397-404(1994).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=10686422; DOI=10.1016/s0945-053x(99)00053-0;
RA Greenhill N.S., Ruger B.M., Hasan Q., Davis P.F.;
RT "The alpha1(VIII) and alpha2(VIII) collagen chains form two distinct
RT homotrimeric proteins in vivo.";
RL Matrix Biol. 19:19-28(2000).
RN [9]
RP FUNCTION OF VASTATIN.
RX PubMed=11708810; DOI=10.1006/bbrc.2001.5970;
RA Xu R., Yao Z.-Y., Xin L., Zhang Q., Li T.-P., Gan R.-B.;
RT "NC1 domain of human type VIII collagen (alpha 1) inhibits bovine aortic
RT endothelial cell proliferation and causes cell apoptosis.";
RL Biochem. Biophys. Res. Commun. 289:264-268(2001).
RN [10]
RP SUBUNIT.
RX PubMed=14990571; DOI=10.1074/jbc.m305805200;
RA Stephan S., Sherratt M.J., Hodson N., Shuttleworth C.A., Kielty C.M.;
RT "Expression and supramolecular assembly of recombinant alpha1(viii) and
RT alpha2(viii) collagen homotrimers.";
RL J. Biol. Chem. 279:21469-21477(2004).
RN [11]
RP INDUCTION.
RX PubMed=17888087; DOI=10.1111/j.1365-2362.2007.01864.x;
RA Gerth J., Cohen C.D., Hopfer U., Lindenmeyer M.T., Sommer M., Grone H.J.,
RA Wolf G.;
RT "Collagen type VIII expression in human diabetic nephropathy.";
RL Eur. J. Clin. Invest. 37:767-773(2007).
CC -!- FUNCTION: Macromolecular component of the subendothelium. Major
CC component of the Descemet's membrane (basement membrane) of corneal
CC endothelial cells. Also a component of the endothelia of blood vessels.
CC Necessary for migration and proliferation of vascular smooth muscle
CC cells and thus, has a potential role in the maintenance of vessel wall
CC integrity and structure, in particular in atherogenesis.
CC {ECO:0000269|PubMed:11708810}.
CC -!- FUNCTION: Vastatin, the C-terminal fragment comprising the NC1 domain,
CC inhibits aortic endothelial cell proliferation and causes cell
CC apoptosis. {ECO:0000269|PubMed:11708810}.
CC -!- SUBUNIT: Homotrimers, or heterotrimers in association with alpha
CC 2(VIII) type collagens. Four homotrimers can form a tetrahedron
CC stabilized by central interacting C-terminal NC1 trimers.
CC {ECO:0000269|PubMed:14990571}.
CC -!- INTERACTION:
CC P27658; Q96C12: ARMC5; NbExp=3; IntAct=EBI-747133, EBI-6425121;
CC P27658; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-747133, EBI-953896;
CC P27658; Q9H5F2: C11orf1; NbExp=3; IntAct=EBI-747133, EBI-718615;
CC P27658; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-747133, EBI-11976299;
CC P27658; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-747133, EBI-7317823;
CC P27658; P48745: CCN3; NbExp=3; IntAct=EBI-747133, EBI-3904822;
CC P27658; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-747133, EBI-747776;
CC P27658; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-747133, EBI-7062247;
CC P27658; Q02930-3: CREB5; NbExp=6; IntAct=EBI-747133, EBI-10192698;
CC P27658; A8MQ03: CYSRT1; NbExp=6; IntAct=EBI-747133, EBI-3867333;
CC P27658; A0A0U1RQF7: DPEP2NB; NbExp=3; IntAct=EBI-747133, EBI-18398199;
CC P27658; Q9NVL1-2: FAM86C1P; NbExp=5; IntAct=EBI-747133, EBI-12845222;
CC P27658; P98095: FBLN2; NbExp=3; IntAct=EBI-747133, EBI-947973;
CC P27658; Q9NWN3: FBXO34; NbExp=3; IntAct=EBI-747133, EBI-719816;
CC P27658; O43559: FRS3; NbExp=3; IntAct=EBI-747133, EBI-725515;
CC P27658; O76003: GLRX3; NbExp=3; IntAct=EBI-747133, EBI-374781;
CC P27658; O15499: GSC2; NbExp=3; IntAct=EBI-747133, EBI-19954058;
CC P27658; P49639: HOXA1; NbExp=6; IntAct=EBI-747133, EBI-740785;
CC P27658; Q0VD86: INCA1; NbExp=9; IntAct=EBI-747133, EBI-6509505;
CC P27658; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-747133, EBI-10693436;
CC P27658; Q5T749: KPRP; NbExp=3; IntAct=EBI-747133, EBI-10981970;
CC P27658; O76014: KRT37; NbExp=3; IntAct=EBI-747133, EBI-1045716;
CC P27658; Q6A162: KRT40; NbExp=3; IntAct=EBI-747133, EBI-10171697;
CC P27658; Q9NSB4: KRT82; NbExp=3; IntAct=EBI-747133, EBI-1045341;
CC P27658; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-747133, EBI-11749135;
CC P27658; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-747133, EBI-10172290;
CC P27658; P60410: KRTAP10-8; NbExp=8; IntAct=EBI-747133, EBI-10171774;
CC P27658; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-747133, EBI-11953334;
CC P27658; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-747133, EBI-10241252;
CC P27658; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-747133, EBI-12196745;
CC P27658; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-747133, EBI-1048945;
CC P27658; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-747133, EBI-10241353;
CC P27658; Q6PEX3: KRTAP26-1; NbExp=4; IntAct=EBI-747133, EBI-3957672;
CC P27658; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-747133, EBI-751260;
CC P27658; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-747133, EBI-10250562;
CC P27658; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-747133, EBI-11987425;
CC P27658; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-747133, EBI-3958099;
CC P27658; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-747133, EBI-11962084;
CC P27658; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-747133, EBI-1044640;
CC P27658; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-747133, EBI-1043191;
CC P27658; P48059-3: LIMS1; NbExp=3; IntAct=EBI-747133, EBI-12864460;
CC P27658; Q3KP22-3: MAJIN; NbExp=3; IntAct=EBI-747133, EBI-18015780;
CC P27658; Q6IA69: NADSYN1; NbExp=3; IntAct=EBI-747133, EBI-748610;
CC P27658; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-747133, EBI-945833;
CC P27658; P0DPK4: NOTCH2NLC; NbExp=5; IntAct=EBI-747133, EBI-22310682;
CC P27658; P32242: OTX1; NbExp=3; IntAct=EBI-747133, EBI-740446;
CC P27658; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-747133, EBI-750734;
CC P27658; Q8WVV4-1: POF1B; NbExp=3; IntAct=EBI-747133, EBI-11986735;
CC P27658; Q12837: POU4F2; NbExp=5; IntAct=EBI-747133, EBI-17236143;
CC P27658; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-747133, EBI-740343;
CC P27658; Q04864: REL; NbExp=3; IntAct=EBI-747133, EBI-307352;
CC P27658; O76081-6: RGS20; NbExp=3; IntAct=EBI-747133, EBI-10178530;
CC P27658; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-747133, EBI-17589229;
CC P27658; P78381-3: SLC35A2; NbExp=3; IntAct=EBI-747133, EBI-13307533;
CC P27658; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-747133, EBI-10269322;
CC P27658; Q02446: SP4; NbExp=3; IntAct=EBI-747133, EBI-10198587;
CC P27658; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-747133, EBI-8635958;
CC P27658; Q9C004: SPRY4; NbExp=3; IntAct=EBI-747133, EBI-354861;
CC P27658; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-747133, EBI-17716262;
CC P27658; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-747133, EBI-947187;
CC P27658; Q08AM6: VAC14; NbExp=7; IntAct=EBI-747133, EBI-2107455;
CC P27658; Q8TCV5: WFDC5; NbExp=3; IntAct=EBI-747133, EBI-12175871;
CC P27658; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-747133, EBI-10251462;
CC P27658; O43257: ZNHIT1; NbExp=3; IntAct=EBI-747133, EBI-347522;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- TISSUE SPECIFICITY: Expressed primarily in the subendothelium of large
CC blood vessels. Also expressed in arterioles and venules in muscle,
CC heart, kidney, spleen, umbilical cord, liver and lung and is also found
CC in connective tissue layers around hair follicles, around nerve bundles
CC in muscle, in the dura of the optic nerve, in cornea and sclera, and in
CC the perichondrium of cartilaginous tissues. In the kidney, expressed in
CC mesangial cells, glomerular endothelial cells, and tubular epithelial
CC cells. Also expressed in mast cells, and in astrocytes during the
CC repair process. Expressed in Descemet's membrane. Specifically
CC expressed in peritoneal fibroblasts and mesothelial cells.
CC {ECO:0000269|PubMed:10686422, ECO:0000269|PubMed:2376131,
CC ECO:0000269|PubMed:7734329}.
CC -!- INDUCTION: Up-regulated during vascular injury, in atherosclerosis and
CC in diabetes. {ECO:0000269|PubMed:17888087}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- PTM: Proteolytically cleaved by neutrophil elastase, in vitro.
CC Proteolytic processing produces the C-terminal NC1 domain fragment,
CC vastatin. {ECO:0000269|PubMed:1515454}.
CC -!- MISCELLANEOUS: Four consecutive Gly-Pro-Pro triplets are present at the
CC C-terminus of the triple-helical region. These may provide the high
CC thermal stability of this region.
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DR EMBL; X57527; CAA40748.1; -; mRNA.
DR EMBL; BT009917; AAP88919.1; -; mRNA.
DR EMBL; CH471052; EAW79837.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79838.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79840.1; -; Genomic_DNA.
DR EMBL; BC013581; AAH13581.1; -; mRNA.
DR CCDS; CCDS2934.1; -.
DR PIR; S15435; S15435.
DR RefSeq; NP_001841.2; NM_001850.4.
DR RefSeq; NP_065084.2; NM_020351.3.
DR AlphaFoldDB; P27658; -.
DR SMR; P27658; -.
DR BioGRID; 107692; 127.
DR ComplexPortal; CPX-1745; Collagen type VIII trimer variant 1.
DR ComplexPortal; CPX-1746; Collagen type VIII trimer variant 2.
DR IntAct; P27658; 72.
DR MINT; P27658; -.
DR STRING; 9606.ENSP00000261037; -.
DR GlyGen; P27658; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P27658; -.
DR PhosphoSitePlus; P27658; -.
DR BioMuta; COL8A1; -.
DR DMDM; 21903375; -.
DR EPD; P27658; -.
DR jPOST; P27658; -.
DR MassIVE; P27658; -.
DR PaxDb; P27658; -.
DR PeptideAtlas; P27658; -.
DR PRIDE; P27658; -.
DR ProteomicsDB; 54404; -.
DR Antibodypedia; 32194; 202 antibodies from 28 providers.
DR DNASU; 1295; -.
DR Ensembl; ENST00000261037.7; ENSP00000261037.3; ENSG00000144810.16.
DR Ensembl; ENST00000273342.8; ENSP00000273342.3; ENSG00000144810.16.
DR Ensembl; ENST00000652472.1; ENSP00000498483.1; ENSG00000144810.16.
DR GeneID; 1295; -.
DR KEGG; hsa:1295; -.
DR MANE-Select; ENST00000652472.1; ENSP00000498483.1; NM_020351.4; NP_065084.2.
DR UCSC; uc003dtg.3; human.
DR CTD; 1295; -.
DR DisGeNET; 1295; -.
DR GeneCards; COL8A1; -.
DR HGNC; HGNC:2215; COL8A1.
DR HPA; ENSG00000144810; Low tissue specificity.
DR MIM; 120251; gene.
DR neXtProt; NX_P27658; -.
DR OpenTargets; ENSG00000144810; -.
DR PharmGKB; PA26731; -.
DR VEuPathDB; HostDB:ENSG00000144810; -.
DR eggNOG; ENOG502QRFR; Eukaryota.
DR GeneTree; ENSGT00940000158272; -.
DR HOGENOM; CLU_001074_21_0_1; -.
DR InParanoid; P27658; -.
DR OMA; KEIPMRS; -.
DR OrthoDB; 1167208at2759; -.
DR PhylomeDB; P27658; -.
DR TreeFam; TF334029; -.
DR PathwayCommons; P27658; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; P27658; -.
DR BioGRID-ORCS; 1295; 11 hits in 1063 CRISPR screens.
DR ChiTaRS; COL8A1; human.
DR GeneWiki; Collagen,_type_VIII,_alpha_1; -.
DR GenomeRNAi; 1295; -.
DR Pharos; P27658; Tbio.
DR PRO; PR:P27658; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P27658; protein.
DR Bgee; ENSG00000144810; Expressed in visceral pleura and 155 other tissues.
DR ExpressionAtlas; P27658; baseline and differential.
DR Genevisible; P27658; HS.
DR GO; GO:0005591; C:collagen type VIII trimer; TAS:ProtInc.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 2.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Basement membrane; Cell adhesion; Collagen;
KW Extracellular matrix; Hydroxylation; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..744
FT /note="Collagen alpha-1(VIII) chain"
FT /id="PRO_0000005762"
FT CHAIN 572..744
FT /note="Vastatin"
FT /id="PRO_0000390484"
FT DOMAIN 611..744
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 29..117
FT /note="Nonhelical region (NC2)"
FT REGION 115..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..571
FT /note="Triple-helical region (COL1)"
FT REGION 459..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..744
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 125..139
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..583
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 262
FT /note="P -> L (in Ref. 1; CAA40748)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="P -> R (in Ref. 1; CAA40748)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="P -> A (in Ref. 1; CAA40748)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="A -> S (in Ref. 1; CAA40748)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="P -> S (in Ref. 1; CAA40748)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="L -> F (in Ref. 1; CAA40748)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="A -> H (in Ref. 1; CAA40748)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="Y -> T (in Ref. 1; CAA40748)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="A -> G (in Ref. 1; CAA40748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 73364 MW; 2BC1B0955DE2C9A3 CRC64;
MAVLPGPLQL LGVLLTISLS SIRLIQAGAY YGIKPLPPQI PPQMPPQIPQ YQPLGQQVPH
MPLAKDGLAM GKEMPHLQYG KEYPHLPQYM KEIQPAPRMG KEAVPKKGKE IPLASLRGEQ
GPRGEPGPRG PPGPPGLPGH GIPGIKGKPG PQGYPGVGKP GMPGMPGKPG AMGMPGAKGE
IGQKGEIGPM GIPGPQGPPG PHGLPGIGKP GGPGLPGQPG PKGDRGPKGL PGPQGLRGPK
GDKGFGMPGA PGVKGPPGMH GPPGPVGLPG VGKPGVTGFP GPQGPLGKPG APGEPGPQGP
IGVPGVQGPP GIPGIGKPGQ DGIPGQPGFP GGKGEQGLPG LPGPPGLPGI GKPGFPGPKG
DRGMGGVPGA LGPRGEKGPI GAPGIGGPPG EPGLPGIPGP MGPPGAIGFP GPKGEGGIVG
PQGPPGPKGE PGLQGFPGKP GFLGEVGPPG MRGLPGPIGP KGEAGQKGVP GLPGVPGLLG
PKGEPGIPGD QGLQGPPGIP GIGGPSGPIG PPGIPGPKGE PGLPGPPGFP GIGKPGVAGL
HGPPGKPGAL GPQGQPGLPG PPGPPGPPGP PAVMPPTPPP QGEYLPDMGL GIDGVKPPHA
YGAKKGKNGG PAYEMPAFTA ELTAPFPPVG APVKFNKLLY NGRQNYNPQT GIFTCEVPGV
YYFAYHVHCK GGNVWVALFK NNEPVMYTYD EYKKGFLDQA SGSAVLLLRP GDRVFLQMPS
EQAAGLYAGQ YVHSSFSGYL LYPM
