ID CO5A2_HUMAN Reviewed; 1499 AA. AC P05997; P78440; Q13908; Q53WR4; Q59GR4; Q6LDJ5; Q7KZ55; Q86XF6; AC Q96QB0; Q96QB3; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 3. DT 09-DEC-2015, entry version 179. DE RecName: Full=Collagen alpha-2(V) chain; DE Flags: Precursor; GN Name=COL5A2; 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 Richards A.J.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-463. RX PubMed=2914927; RA Woodbury D., Benson-Chanda V., Ramirez F.; RT "Amino-terminal propeptide of human pro-alpha 2(V) collagen conforms RT to the structural criteria of a fibrillar procollagen molecule."; RL J. Biol. Chem. 264:2735-2738(1989). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104 AND 153-1499. RX PubMed=11566270; DOI=10.1016/S0945-053X(01)00145-7; RA Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G., RA Ala-Kokko L.; RT "Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has RT evolved differently than the other minor fibrillar collagen genes."; RL Matrix Biol. 20:357-366(2001). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. RX PubMed=1820205; RA Greenspan D.S., Lee S.T., Lee B.S., Hoffman G.G.; RT "Homology between alpha 2(V) and alpha 1(III) collagen promoters and RT evidence for negatively acting elements in the alpha 2(V) first intron RT and 5' flanking sequences."; RL Gene Expr. 1:29-39(1991). RN [7] RP PROTEIN SEQUENCE OF 208-227. RC TISSUE=Placenta; RX PubMed=1571108; RA Mann K.; RT "Isolation of the alpha 3-chain of human type V collagen and RT characterization by partial sequencing."; RL Biol. Chem. Hoppe-Seyler 373:69-75(1992). RN [8] RP PROTEIN SEQUENCE OF 288-297 AND 609-620, AND HYDROXYLATION AT PRO-290; RP PRO-293; PRO-296; PRO-611 AND PRO-617. RC TISSUE=Bone; RX PubMed=8181482; DOI=10.1111/j.1432-1033.1994.tb18815.x; RA Moradi-Ameli M., Rousseau J.C., Kleman J.P., Champliaud M.-F., RA Boutillon M.-M., Bernillon J., Wallach J.M., van der Rest M.; RT "Diversity in the processing events at the N-terminus of type-V RT collagen."; RL Eur. J. Biochem. 221:987-995(1994). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 398-1499. RX PubMed=3029669; DOI=10.1093/nar/15.1.181; RA Weil D., Bernard M.P., Gargano S., Ramirez F.; RT "The pro alpha 2(V) collagen gene is evolutionarily related to the RT major fibrillar-forming collagens."; RL Nucleic Acids Res. 15:181-198(1987). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 878-1499. RC TISSUE=Skin; 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 [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1229, AND PROTEIN SEQUENCE OF RP 1006-1036. RX PubMed=2985598; RA Myers J.C., Loidl H.R., Stolle C.A., Seyer J.M.; RT "Partial covalent structure of the human alpha 2 type V collagen RT chain."; RL J. Biol. Chem. 260:5533-5541(1985). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1006-1037. RX PubMed=3858826; DOI=10.1073/pnas.82.10.3385; RA Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C.; RT "Human alpha 1(III) and alpha 2(V) procollagen genes are located on RT the long arm of chromosome 2."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1230-1499. RX PubMed=2411731; RA Myers J.C., Loidl H.R., Seyer J.M., Dion A.S.; RT "Complete primary structure of the human alpha 2 type V procollagen RT COOH-terminal propeptide."; RL J. Biol. Chem. 260:11216-11222(1985). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1452-1499. RX PubMed=3224983; DOI=10.1016/0888-7543(88)90089-4; RA Tsipouras P., Schwartz R.C., Liddell A.C., Salkeld C.S., Weil D., RA Ramirez F.; RT "Genetic distance of two fibrillar collagen loci, COL3A1 and COL5A2, RT located on the long arm of human chromosome 2."; RL Genomics 3:275-277(1988). RN [15] RP INVOLVEMENT IN EDS. RX PubMed=9425231; DOI=10.1093/hmg/7.2.249; RA Michalickova K., Susic M., Willing M.C., Wenstrup R.J., Cole W.G.; RT "Mutations of the alpha2(V) chain of type V collagen impair matrix RT assembly and produce Ehlers-Danlos syndrome type I."; RL Hum. Mol. Genet. 7:249-255(1998). RN [16] RP HYDROXYLATION AT PRO-919 AND PRO-1156, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=21757687; DOI=10.1074/jbc.M111.267906; RA Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.; RT "A role for prolyl 3-hydroxylase 2 in post-translational modification RT of fibril-forming collagens."; RL J. Biol. Chem. 286:30662-30669(2011). RN [17] RP VARIANT EDS ARG-963. RX PubMed=9783710; DOI=10.1136/jmg.35.10.846; RA Richards A.J., Martin S., Nicholls A.C., Harrison J.B., Pope F.M., RA Burrows N.P.; RT "A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type RT II."; RL J. Med. Genet. 35:846-848(1998). RN [18] RP VARIANTS ALA-512; LEU-833; SER-1230 AND VAL-1432. RX PubMed=11940702; DOI=10.1212/WNL.58.7.1103; RA Grond-Ginsbach C., Wigger F., Morcher M., von Pein F., Grau A., RA Hausser I., Brandt T.; RT "Sequence analysis of the COL5A2 gene in patients with spontaneous RT cervical artery dissections."; RL Neurology 58:1103-1105(2002). CC -!- FUNCTION: Type V collagen is a member of group I collagen CC (fibrillar forming collagen). It is a minor connective tissue CC component of nearly ubiquitous distribution. Type V collagen binds CC to DNA, heparan sulfate, thrombospondin, heparin, and insulin. CC Type V collagen is a key determinant in the assembly of tissue- CC specific matrices (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains in CC most tissues and trimers of one alpha 1(V), one alpha 2(V), and CC one alpha 3(V) chains in placenta. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, CC have crucial roles in tissue growth and repair by controlling both CC the intracellular assembly of procollagen molecules and the CC extracellular assembly of collagen fibrils. It binds a calcium ion CC which is essential for its function (By similarity). CC {ECO:0000250}. CC -!- PTM: Prolines at the third position of the tripeptide repeating CC unit (G-X-P) are hydroxylated in some or all of the chains. CC Probably 3-hydroxylated on Pro-919 and Pro-1156 by LEPREL1. CC {ECO:0000269|PubMed:21757687, ECO:0000269|PubMed:8181482}. CC -!- DISEASE: Ehlers-Danlos syndrome, classic type (EDS) [MIM:130000]: CC A connective tissue disorder characterized by hyperextensible CC skin, atrophic cutaneous scars due to tissue fragility and joint CC hyperlaxity. {ECO:0000269|PubMed:9425231, CC ECO:0000269|PubMed:9783710}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- SIMILARITY: Contains 1 fibrillar collagen NC1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- SIMILARITY: Contains 1 VWFC domain. {ECO:0000255|PROSITE- CC ProRule:PRU00220}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH43613.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAY24185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAD92282.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y14690; CAA75002.1; -; mRNA. DR EMBL; AB209045; BAD92282.1; ALT_INIT; mRNA. DR EMBL; AC064833; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC133106; AAY24185.1; ALT_SEQ; Genomic_DNA. DR EMBL; J04478; AAA51859.1; -; mRNA. DR EMBL; AY016288; AAL13165.1; -; Genomic_DNA. DR EMBL; AY016287; AAL13165.1; JOINED; Genomic_DNA. DR EMBL; AY016295; AAL13166.1; -; Genomic_DNA. DR EMBL; AY016289; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016290; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016291; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016292; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016293; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016294; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; M58529; AAC41699.1; -; Genomic_DNA. DR EMBL; X04758; CAA28454.1; -; mRNA. DR EMBL; BC043613; AAH43613.1; ALT_INIT; mRNA. DR EMBL; M10956; AAA52007.1; -; mRNA. DR EMBL; M11135; AAA51857.1; -; mRNA. DR EMBL; M11718; AAA52058.1; -; mRNA. DR EMBL; J03051; AAA51858.1; -; Genomic_DNA. DR CCDS; CCDS33350.1; -. DR PIR; A31427; CGHU2V. DR RefSeq; NP_000384.2; NM_000393.3. DR UniGene; Hs.445827; -. DR PDB; 1A9A; Model; -; B=561-581. DR PDBsum; 1A9A; -. DR ProteinModelPortal; P05997; -. DR SMR; P05997; 1284-1499. DR IntAct; P05997; 2. DR STRING; 9606.ENSP00000364000; -. DR ChEMBL; CHEMBL2364188; -. DR PhosphoSite; P05997; -. DR BioMuta; COL5A2; -. DR DMDM; 143811378; -. DR MaxQB; P05997; -. DR PaxDb; P05997; -. DR PRIDE; P05997; -. DR Ensembl; ENST00000374866; ENSP00000364000; ENSG00000204262. DR GeneID; 1290; -. DR KEGG; hsa:1290; -. DR UCSC; uc002uqk.3; human. DR CTD; 1290; -. DR GeneCards; COL5A2; -. DR GeneReviews; COL5A2; -. DR HGNC; HGNC:2210; COL5A2. DR MalaCards; COL5A2; -. DR MIM; 120190; gene. DR MIM; 130000; phenotype. DR neXtProt; NX_P05997; -. DR Orphanet; 90309; Ehlers-Danlos syndrome type 1. DR Orphanet; 90318; Ehlers-Danlos syndrome type 2. DR PharmGKB; PA26725; -. DR eggNOG; KOG3544; Eukaryota. DR eggNOG; ENOG4110XTV; LUCA. DR GeneTree; ENSGT00820000126960; -. DR HOVERGEN; HBG004933; -. DR InParanoid; P05997; -. DR KO; K06236; -. DR OMA; IGIRGQP; -. DR OrthoDB; EOG7TJ3HH; -. DR PhylomeDB; P05997; -. DR TreeFam; TF344135; -. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1474244; Extracellular matrix organization. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-186797; Signaling by PDGF. 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-3000170; Syndecan interactions. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-419037; NCAM1 interactions. DR ChiTaRS; COL5A2; human. DR GeneWiki; COL5A2; -. DR GenomeRNAi; 1290; -. DR NextBio; 5223; -. DR PMAP-CutDB; P05997; -. DR PRO; PR:P05997; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; P05997; -. DR ExpressionAtlas; P05997; baseline and differential. DR Genevisible; P05997; HS. DR GO; GO:0005588; C:collagen type V trimer; IMP:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0030574; P:collagen catabolic process; TAS:Reactome. DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0048592; P:eye morphogenesis; IMP:UniProtKB. DR GO; GO:1903225; P:negative regulation of endodermal cell differentiation; IDA:UniProtKB. DR GO; GO:0001503; P:ossification; IEA:Ensembl. DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl. DR GO; GO:0043588; P:skin development; IMP:UniProtKB. DR InterPro; IPR008160; Collagen. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR001007; VWF_dom. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 5. DR Pfam; PF00093; VWC; 1. DR ProDom; PD002078; Fib_collagen_C; 1. DR SMART; SM00038; COLFI; 1. DR SMART; SM00214; VWC; 1. DR PROSITE; PS51461; NC1_FIB; 1. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Collagen; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; KW Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; KW Hydroxylation; Metal-binding; Polymorphism; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1 26 FT CHAIN 27 1229 Collagen alpha-2(V) chain. FT /FTId=PRO_0000005830. FT PROPEP 1230 1499 C-terminal propeptide. FT /FTId=PRO_0000005831. FT DOMAIN 39 97 VWFC. {ECO:0000255|PROSITE- FT ProRule:PRU00220}. FT DOMAIN 1266 1499 Fibrillar collagen NC1. FT {ECO:0000255|PROSITE-ProRule:PRU00793}. FT MOTIF 506 508 Cell attachment site. {ECO:0000255}. FT MOTIF 944 946 Cell attachment site. {ECO:0000255}. FT MOTIF 1067 1069 Cell attachment site. {ECO:0000255}. FT MOTIF 1070 1072 Cell attachment site. {ECO:0000255}. FT MOTIF 1100 1102 Cell attachment site. {ECO:0000255}. FT MOTIF 1127 1129 Cell attachment site. {ECO:0000255}. FT MOTIF 1136 1138 Cell attachment site. {ECO:0000255}. FT METAL 1314 1314 Calcium. {ECO:0000250}. FT METAL 1316 1316 Calcium. {ECO:0000250}. FT METAL 1317 1317 Calcium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 1322 1322 Calcium. {ECO:0000250}. FT MOD_RES 290 290 Hydroxyproline. FT {ECO:0000269|PubMed:8181482}. FT MOD_RES 293 293 Hydroxyproline. FT {ECO:0000269|PubMed:8181482}. FT MOD_RES 296 296 Hydroxyproline. FT {ECO:0000269|PubMed:8181482}. FT MOD_RES 611 611 Hydroxyproline. FT {ECO:0000269|PubMed:8181482}. FT MOD_RES 617 617 Hydroxyproline. FT {ECO:0000269|PubMed:8181482}. FT MOD_RES 919 919 3-hydroxyproline; partial. FT {ECO:0000269|PubMed:21757687}. FT MOD_RES 1156 1156 3-hydroxyproline; partial. FT {ECO:0000269|PubMed:21757687}. FT CARBOHYD 1262 1262 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 1400 1400 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 1296 1328 {ECO:0000255|PROSITE-ProRule:PRU00793}. FT DISULFID 1336 1497 {ECO:0000255|PROSITE-ProRule:PRU00793}. FT DISULFID 1405 1450 {ECO:0000255|PROSITE-ProRule:PRU00793}. FT VARIANT 460 460 P -> S (in dbSNP:rs35830636). FT /FTId=VAR_048799. FT VARIANT 512 512 V -> A (in dbSNP:rs35852101). FT {ECO:0000269|PubMed:11940702}. FT /FTId=VAR_057910. FT VARIANT 833 833 P -> L (in dbSNP:rs116298748). FT {ECO:0000269|PubMed:11940702}. FT /FTId=VAR_057911. FT VARIANT 956 956 R -> P (in dbSNP:rs6434313). FT /FTId=VAR_048800. FT VARIANT 963 963 G -> R (in EDS). FT {ECO:0000269|PubMed:9783710}. FT /FTId=VAR_013588. FT VARIANT 1230 1230 T -> S. {ECO:0000269|PubMed:11940702}. FT /FTId=VAR_057912. FT VARIANT 1432 1432 D -> V. {ECO:0000269|PubMed:11940702}. FT /FTId=VAR_057913. FT CONFLICT 292 292 A -> P (in Ref. 8; AA sequence). FT {ECO:0000305}. FT CONFLICT 361 361 M -> L (in Ref. 5; AAL13166). FT {ECO:0000305}. FT CONFLICT 430 430 A -> P (in Ref. 1; CAA75002, 4; AAA51859 FT and 9; CAA28454). {ECO:0000305}. FT CONFLICT 463 466 IRGQ -> NSGL (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 463 463 I -> N (in Ref. 4; AAA51859). FT {ECO:0000305}. FT CONFLICT 472 474 Missing (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 512 512 V -> L (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 608 608 R -> K (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 613 613 S -> T (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 623 623 S -> N (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 635 635 A -> P (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 649 649 E -> K (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 653 653 S -> Y (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 656 656 V -> P (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 662 662 A -> R (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 679 679 L -> H (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 700 700 D -> G (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 797 797 R -> G (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 811 812 PT -> LL (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 853 853 P -> S (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 943 943 L -> P (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 955 955 D -> V (in Ref. 1; CAA75002 and 9; FT CAA28454). {ECO:0000305}. FT CONFLICT 1111 1112 PP -> HL (in Ref. 1; CAA75002, 9; FT CAA28454 and 11; AAA52007). FT {ECO:0000305}. FT CONFLICT 1196 1196 I -> L (in Ref. 1; CAA75002, 9; CAA28454 FT and 11; AAA52007). {ECO:0000305}. FT CONFLICT 1421 1421 K -> T (in Ref. 13; AAA52058). FT {ECO:0000305}. FT CONFLICT 1441 1441 F -> S (in Ref. 13; AAA52058). FT {ECO:0000305}. FT CONFLICT 1467 1467 Q -> E (in Ref. 14; AAA51858). FT {ECO:0000305}. SQ SEQUENCE 1499 AA; 144910 MW; E8C92BF5E749EC97 CRC64; MMANWAEARP LLILIVLLGQ FVSIKAQEED EDEGYGEEIA CTQNGQMYLN RDIWKPAPCQ ICVCDNGAIL CDKIECQDVL DCADPVTPPG ECCPVCSQTP GGGNTNFGRG RKGQKGEPGL VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG RPGPRGPQGI DGEPGVPGQP GAPGPPGHPS HPGPDGLSRP FSAQMAGLDE KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGAGPTGPPG EPGDPGPMGP IGSRGPEGPP GKPGEDGEPG RNGNPGEVGF AGSPGARGFP GAPGLPGLKG HRGHKGLEGP KGEVGAPGSK GEAGPTGPMG AMGPLGPRGM PGERGRLGPQ GAPGQRGAHG MPGKPGPMGP LGIPGSSGFP GNPGMKGEAG PTGARGPEGP QGQRGETGPP GPVGSPGLPG AIGTDGTPGA KGPTGSPGTS GPPGSAGPPG SPGPQGSTGP QGIRGQPGDP GVPGFKGEAG PKGEPGPHGI QGPIGPPGEE GKRGPRGDPG TVGPPGPVGE RGAPGNRGFP GSDGLPGPKG AQGERGPVGS SGPKGSQGDP GRPGEPGLPG ARGLTGNPGV QGPEGKLGPL GAPGEDGRPG PPGSIGIRGQ PGSMGLPGPK GSSGDPGKPG EAGNAGVPGQ RGAPGKDGEV GPSGPVGPPG LAGERGEQGP PGPTGFQGLP GPPGPPGEGG KPGDQGVPGD PGAVGPLGPR GERGNPGERG EPGITGLPGE KGMAGGHGPD GPKGSPGPSG TPGDTGPPGL QGMPGERGIA GTPGPKGDRG GIGEKGAEGT AGNDGARGLP GPLGPPGPAG PTGEKGEPGP RGLVGPPGSR GNPGSRGENG PTGAVGFAGP QGPDGQPGVK GEPGEPGQKG DAGSPGPQGL AGSPGPHGPN GVPGLKGGRG TQGPPGATGF PGSAGRVGPP GPAGAPGPAG PLGEPGKEGP PGLRGDPGSH GRVGDRGPAG PPGGPGDKGD PGEDGQPGPD GPPGPAGTTG QRGIVGMPGQ RGERGMPGLP GPAGTPGKVG PTGATGDKGP PGPVGPPGSN GPVGEPGPEG PAGNDGTPGR DGAVGERGDR GDPGPAGLPG SQGAPGTPGP VGAPGDAGQR GDPGSRGPIG PPGRAGKRGL PGPQGPRGDK GDHGDRGDRG QKGHRGFTGL QGLPGPPGPN GEQGSAGIPG PFGPRGPPGP VGPSGKEGNP GPLGPIGPPG VRGSVGEAGP EGPPGEPGPP GPPGPPGHLT AALGDIMGHY DESMPDPLPE FTEDQAAPDD KNKTDPGVHA TLKSLSSQIE TMRSPDGSKK HPARTCDDLK LCHSAKQSGE YWIDPNQGSV EDAIKVYCNM ETGETCISAN PSSVPRKTWW ASKSPDNKPV WYGLDMNRGS QFAYGDHQSP NTAITQMTFL RLLSKEASQN ITYICKNSVG YMDDQAKNLK KAVVLKGAND LDIKAEGNIR FRYIVLQDTC SKRNGNVGKT VFEYRTQNVA RLPIIDLAPV DVGGTDQEFG VEIGPVCFV //