ID COEA1_HUMAN Reviewed; 1796 AA. AC Q05707; B2RU07; O00260; O00261; O00262; Q05708; Q5XJ18; Q96C67; Q9UDF6; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 3. DT 27-NOV-2024, entry version 189. DE RecName: Full=Collagen alpha-1(XIV) chain; DE AltName: Full=Undulin; DE Flags: Precursor; GN Name=COL14A1 {ECO:0000312|HGNC:HGNC:2191}; Synonyms=UND; 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH83495.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-1342. RC TISSUE=Brain, Muscle {ECO:0000312|EMBL:AAH14640.1}, and PNS RC {ECO:0000312|EMBL:AAH83495.1}; 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 [3] {ECO:0000305, ECO:0000312|EMBL:CAA72402.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-165, NUCLEOTIDE SEQUENCE [MRNA] OF RP 1026-1796 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA] OF 1760-1796 (ISOFORM RP 2). RX PubMed=9427527; DOI=10.1016/s0167-4781(97)00131-0; RA Bauer M., Dieterich W., Ehnis T., Schuppan D.; RT "Complete primary structure of human collagen type XIV (undulin)."; RL Biochim. Biophys. Acta 1354:183-188(1997). RN [4] {ECO:0000305, ECO:0000312|EMBL:AAA36794.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 149-582 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE RP [MRNA] OF 188-1030 (ISOFORM 1). RX PubMed=1716629; DOI=10.1016/s0021-9258(19)47377-8; RA Just M., Herbst H., Hummel M., Duerkop H., Tripier D., Stein H., RA Schuppan D.; RT "Undulin is a novel member of the fibronectin-tenascin family of RT extracellular matrix glycoproteins."; RL J. Biol. Chem. 266:17326-17332(1991). RN [5] RP PROTEIN SEQUENCE OF 1459-1635 AND 1640-1767, HYDROXYLATION AT PRO-1467; RP PRO-1470; LYS-1476; PRO-1482; LYS-1485; PRO-1497; PRO-1503; PRO-1517; RP PRO-1520; LYS-1523; LYS-1526; PRO-1532; PRO-1538; PRO-1544; PRO-1550; RP PRO-1556; PRO-1565; PRO-1568; PRO-1574; PRO-1577; PRO-1580; PRO-1595; RP PRO-1598; LYS-1601; PRO-1643; PRO-1656; PRO-1659; PRO-1662; PRO-1665; RP PRO-1668; PRO-1674; PRO-1677; PRO-1680; PRO-1686; PRO-1689; LYS-1698; RP LYS-1701; PRO-1704; PRO-1715; PRO-1726; PRO-1729; PRO-1732; PRO-1735; RP PRO-1741; PRO-1747 AND PRO-1756, AND GLYCOSYLATION AT LYS-1476; LYS-1485; RP LYS-1523; LYS-1526; LYS-1601; LYS-1698 AND LYS-1701. RC TISSUE=Placenta; RX PubMed=7827751; DOI=10.1016/0945-053x(94)90194-5; RA Brown J.C., Golbik R., Mann K., Timpl R.; RT "Structure and stability of the triple-helical domains of human collagen RT XIV."; RL Matrix Biol. 14:287-295(1994). RN [6] {ECO:0000305} RP FUNCTION. RX PubMed=2187872; DOI=10.1016/s0021-9258(19)38962-8; RA Schuppan D., Cantaluppi M., Becker J., Veit A., Bunte T., Troyer D., RA Schuppan F., Schmid M., Ackermann R., Hahn E.; RT "Undulin, an extracellular matrix glycoprotein associated with collagen RT fibrils."; RL J. Biol. Chem. 265:8823-8832(1990). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94; ASN-372; ASN-1384 AND RP ASN-1388. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Plays an adhesive role by integrating collagen bundles. It is CC probably associated with the surface of interstitial collagen fibrils CC via COL1. The COL2 domain may then serve as a rigid arm which sticks CC out from the fibril and protrudes the large N-terminal globular domain CC into the extracellular space, where it might interact with other matrix CC molecules or cell surface receptors (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:2187872}. CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P32018}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250|UniProtKB:P32018}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1 {ECO:0000269|PubMed:9427527}; Synonyms=Undulin 1 CC {ECO:0000303|PubMed:1716629}, Un1 {ECO:0000303|PubMed:1716629}; CC IsoId=Q05707-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:9427527}; CC IsoId=Q05707-2; Sequence=VSP_051654; CC Name=3 {ECO:0000269|PubMed:1716629}; Synonyms=Undulin 2 CC {ECO:0000303|PubMed:1716629}, Un2 {ECO:0000303|PubMed:1716629}; CC IsoId=Q05707-3; Sequence=VSP_051653; CC -!- PTM: Lysines at the third position of the tripeptide repeating unit (G- CC X-Y) are hydroxylated in all cases and bind carbohydrates. CC {ECO:0000250|UniProtKB:P32018}. 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 {ECO:0000250|UniProtKB:P32018}. CC -!- PTM: May contain numerous cysteine residues involved in inter- and CC intramolecular disulfide bonding. {ECO:0000250|UniProtKB:P32018}. CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted CC helices (FACIT) family. {ECO:0000255}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA36795.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305}; CC Sequence=AAH14640.1; Type=Frameshift; 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; AC020603; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090735; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107877; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014640; AAH14640.1; ALT_FRAME; mRNA. DR EMBL; BC083495; AAH83495.1; -; mRNA. DR EMBL; BC140893; AAI40894.1; -; mRNA. DR EMBL; Y11709; CAA72401.1; -; mRNA. DR EMBL; Y11710; CAA72402.1; -; mRNA. DR EMBL; Y11711; CAA72403.1; -; mRNA. DR EMBL; M64108; AAA36794.1; -; mRNA. DR EMBL; M64109; AAA36795.1; ALT_SEQ; mRNA. DR CCDS; CCDS34938.1; -. [Q05707-1] DR CCDS; CCDS94338.1; -. [Q05707-2] DR PIR; A40970; A40970. DR PIR; B40970; B40970. DR PIR; S37749; S37749. DR PIR; S46657; S46657. DR RefSeq; NP_066933.1; NM_021110.3. [Q05707-1] DR RefSeq; XP_005251116.1; XM_005251059.3. DR RefSeq; XP_006716714.1; XM_006716651.3. DR RefSeq; XP_016869298.1; XM_017013809.1. DR AlphaFoldDB; Q05707; -. DR SMR; Q05707; -. DR BioGRID; 113219; 86. DR ComplexPortal; CPX-1755; Collagen type XIV trimer. DR IntAct; Q05707; 69. DR STRING; 9606.ENSP00000297848; -. DR GlyConnect; 1132; 18 N-Linked glycans (4 sites). DR GlyCosmos; Q05707; 18 sites, 24 glycans. DR GlyGen; Q05707; 23 sites, 97 N-linked glycans (4 sites), 9 O-linked glycans (11 sites). DR iPTMnet; Q05707; -. DR PhosphoSitePlus; Q05707; -. DR BioMuta; COL14A1; -. DR DMDM; 125987815; -. DR jPOST; Q05707; -. DR MassIVE; Q05707; -. DR PaxDb; 9606-ENSP00000297848; -. DR PeptideAtlas; Q05707; -. DR ProteomicsDB; 58350; -. [Q05707-1] DR ProteomicsDB; 58351; -. [Q05707-2] DR ProteomicsDB; 58352; -. [Q05707-3] DR Pumba; Q05707; -. DR Antibodypedia; 13712; 115 antibodies from 23 providers. DR DNASU; 7373; -. DR Ensembl; ENST00000297848.8; ENSP00000297848.3; ENSG00000187955.13. [Q05707-1] DR Ensembl; ENST00000309791.8; ENSP00000311809.4; ENSG00000187955.13. [Q05707-2] DR GeneID; 7373; -. DR KEGG; hsa:7373; -. DR MANE-Select; ENST00000297848.8; ENSP00000297848.3; NM_021110.4; NP_066933.1. DR UCSC; uc003yox.5; human. [Q05707-1] DR AGR; HGNC:2191; -. DR CTD; 7373; -. DR DisGeNET; 7373; -. DR GeneCards; COL14A1; -. DR HGNC; HGNC:2191; COL14A1. DR HPA; ENSG00000187955; Tissue enhanced (cervix). DR MalaCards; COL14A1; -. DR MIM; 120324; gene. DR neXtProt; NX_Q05707; -. DR OpenTargets; ENSG00000187955; -. DR Orphanet; 79501; Punctate palmoplantar keratoderma type 1. DR PharmGKB; PA26707; -. DR VEuPathDB; HostDB:ENSG00000187955; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000153769; -. DR HOGENOM; CLU_002527_2_0_1; -. DR InParanoid; Q05707; -. DR OMA; REMQSDX; -. DR OrthoDB; 5353225at2759; -. DR PhylomeDB; Q05707; -. DR TreeFam; TF329914; -. DR PathwayCommons; Q05707; -. 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-8948216; Collagen chain trimerization. DR SignaLink; Q05707; -. DR SIGNOR; Q05707; -. DR BioGRID-ORCS; 7373; 12 hits in 1150 CRISPR screens. DR ChiTaRS; COL14A1; human. DR GeneWiki; Collagen,_type_XIV,_alpha_1; -. DR GenomeRNAi; 7373; -. DR Pharos; Q05707; Tbio. DR PRO; PR:Q05707; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q05707; protein. DR Bgee; ENSG00000187955; Expressed in descending thoracic aorta and 169 other cell types or tissues. DR ExpressionAtlas; Q05707; baseline and differential. DR GO; GO:0005581; C:collagen trimer; NAS:UniProtKB. DR GO; GO:0005596; C:collagen type XIV trimer; NAS:UniProtKB. 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; NAS:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:0005614; C:interstitial matrix; IBA:GO_Central. DR GO; GO:0005518; F:collagen binding; NAS:UniProtKB. DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; ISS:BHF-UCL. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB. DR GO; GO:0030199; P:collagen fibril organization; NAS:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; NAS:UniProtKB. DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl. DR GO; GO:0061050; P:regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl. DR GO; GO:0003229; P:ventricular cardiac muscle tissue development; IEA:Ensembl. DR CDD; cd00063; FN3; 8. DR CDD; cd01482; vWA_collagen_alphaI-XII-like; 2. DR FunFam; 2.60.40.10:FF:000444; Collagen alpha-1(XIV) chain isoform X2; 1. DR FunFam; 2.60.40.10:FF:000514; Collagen alpha-1(XIV) chain isoform X2; 1. DR FunFam; 2.60.40.10:FF:000546; Collagen alpha-1(XIV) chain isoform X2; 1. DR FunFam; 2.60.40.10:FF:000403; collagen alpha-1(XIV) chain isoform X2; 1. DR FunFam; 2.60.40.10:FF:000615; collagen alpha-1(XIV) chain isoform X2; 1. DR FunFam; 2.60.40.10:FF:000656; collagen alpha-1(XIV) chain isoform X2; 1. DR FunFam; 2.60.120.200:FF:000008; Collagen type XII alpha 1 chain; 1. DR FunFam; 2.60.40.10:FF:000234; Collagen, type XII, alpha 1; 2. DR FunFam; 3.40.50.410:FF:000001; Collagen, type XII, alpha 1; 2. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 8. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2. DR InterPro; IPR008160; Collagen. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR050525; ECM_Assembly_Org. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR048287; TSPN-like_N. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24020:SF15; COLLAGEN ALPHA-1(XIV) CHAIN; 1. DR Pfam; PF01391; Collagen; 4. DR Pfam; PF00041; fn3; 7. DR Pfam; PF00092; VWA; 2. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00060; FN3; 8. DR SMART; SM00210; TSPN; 1. DR SMART; SM00327; VWA; 2. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF49265; Fibronectin type III; 5. DR SUPFAM; SSF53300; vWA-like; 2. DR PROSITE; PS50853; FN3; 8. DR PROSITE; PS50234; VWFA; 2. PE 1: Evidence at protein level; KW Alternative splicing; Cell adhesion; Collagen; Direct protein sequencing; KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation; KW Proteomics identification; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT CHAIN 29..1796 FT /note="Collagen alpha-1(XIV) chain" FT /id="PRO_0000005785" FT DOMAIN 32..122 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 158..330 FT /note="VWFA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 355..444 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 445..536 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 537..626 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 627..715 FT /note="Fibronectin type-III 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 737..829 FT /note="Fibronectin type-III 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 831..921 FT /note="Fibronectin type-III 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 922..1010 FT /note="Fibronectin type-III 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1032..1205 FT /note="VWFA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 1229..1424 FT /note="Laminin G-like" FT DOMAIN 1462..1510 FT /note="Collagen-like 1" FT DOMAIN 1514..1570 FT /note="Collagen-like 2" FT DOMAIN 1571..1609 FT /note="Collagen-like 3" FT DOMAIN 1653..1705 FT /note="Collagen-like 4" FT REGION 124..145 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1217..1458 FT /note="Nonhelical region (NC4)" FT REGION 1459..1610 FT /note="Triple-helical region 1 (COL2)" FT REGION 1462..1613 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1644..1781 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1654..1779 FT /note="Triple-helical region 2 (COL1)" FT MOTIF 1607..1609 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 1561..1575 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1658..1675 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1710..1747 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1467 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1470 FT /note="4-hydroxyproline; partial" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1476 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1482 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1485 FT /note="5-hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1497 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1503 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1517 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1520 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1523 FT /note="5-hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1526 FT /note="5-hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1532 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1538 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1544 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1550 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1556 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1565 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1568 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1574 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1577 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1580 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1595 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1598 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1601 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1643 FT /note="4-hydroxyproline; partial" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1656 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1659 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1662 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1665 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1668 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1674 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1677 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1680 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1686 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1689 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1698 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1701 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1704 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1715 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1726 FT /note="4-hydroxyproline; partial" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1729 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1732 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1735 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1741 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1747 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT MOD_RES 1756 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7827751" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 137 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 372 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1384 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1388 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1476 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:7827751" FT CARBOHYD 1485 FT /note="O-linked (Gal...) hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:7827751" FT CARBOHYD 1523 FT /note="O-linked (Gal...) hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:7827751" FT CARBOHYD 1526 FT /note="O-linked (Gal...) hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:7827751" FT CARBOHYD 1601 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:7827751" FT CARBOHYD 1698 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:7827751" FT CARBOHYD 1701 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:7827751" FT VAR_SEQ 197..291 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:1716629" FT /id="VSP_051653" FT VAR_SEQ 1771..1796 FT /note="APHPDQPEFTPVQDELEAMELWGPGV -> DLIPYNDYQH (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:9427527" FT /id="VSP_051654" FT VARIANT 563 FT /note="N -> H (in dbSNP:rs4870723)" FT /id="VAR_048772" FT VARIANT 636 FT /note="T -> A (in dbSNP:rs56815167)" FT /id="VAR_061113" FT VARIANT 855 FT /note="P -> L (in dbSNP:rs2305606)" FT /id="VAR_048773" FT VARIANT 922 FT /note="V -> I (in dbSNP:rs11774228)" FT /id="VAR_048774" FT VARIANT 1342 FT /note="V -> L (in dbSNP:rs17833992)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_048775" FT CONFLICT 616 FT /note="T -> I (in Ref. 2; AAA36794)" FT /evidence="ECO:0000305" FT CONFLICT 1025 FT /note="V -> G (in Ref. 2; AAA36794)" FT /evidence="ECO:0000305" SQ SEQUENCE 1796 AA; 193515 MW; 30A72F6E2CC07F70 CRC64; MKIFQRKMRY WLLPPFLAIV YFCTIVQGQV APPTRLRYNV ISHDSIQISW KAPRGKFGGY KLLVTPTSGG KTNQLNLQNT ATKAIIQGLM PDQNYTVQII AYNKDKESKP AQGQFRIKDL EKRKDPKPRV KVVDRGNGSR PSSPEEVKFV CQTPAIADIV ILVDGSWSIG RFNFRLVRHF LENLVTAFDV GSEKTRIGLA QYSGDPRIEW HLNAFSTKDE VIEAVRNLPY KGGNTLTGLA LNYIFENSFK PEAGSRTGVS KIGILITDGK SQDDIIPPSR NLRESGVELF AIGVKNADVN ELQEIASEPD STHVYNVAEF DLMHTVVESL TRTLCSRVEE QDREIKASAH AITGPPTELI TSEVTARSFM VNWTHAPGNV EKYRVVYYPT RGGKPDEVVV DGTVSSTVLK NLMSLTEYQI AVFAIYAHTA SEGLRGTETT LALPMASDLL LYDVTENSMR VKWDAVPGAS GYLILYAPLT EGLAGDEKEM KIGETHTDIE LSGLLPNTEY TVTVYAMFGE EASDPVTGQE TTLALSPPRN LRISNVGSNS ARLTWDPTSR QINGYRIVYN NADGTEINEV EVDPITTFPL KGLTPLTEYT IAIFSIYDEG QSEPLTGVFT TEEVPAQQYL EIDEVTTDSF RVTWHPLSAD EGLHKLMWIP VYGGKTEEVV LKEEQDSHVI EGLEPGTEYE VSLLAVLDDG SESEVVTAVG TTLDSFWTEP ATTIVPTTSV TSVFQTGIRN LVVGDETTSS LRVKWDISDS DVQQFRVTYM TAQGDPEEEV IGTVMVPGSQ NNLLLKPLLP DTEYKVTVTP IYTDGEGVSV SAPGKTLPSS GPQNLRVSEE WYNRLRITWD PPSSPVKGYR IVYKPVSVPG PTLETFVGAD INTILITNLL SGMDYNVKIF ASQASGFSDA LTGMVKTLFL GVTNLQAKHV EMTSLCAHWQ VHRHATAYRV VIESLQDRQK QESTVGGGTT RHCFYGLQPD SEYKISVYTK LQEIEGPSVS IMEKTQSLPT RPPTFPPTIP PAKEVCKAAK ADLVFMVDGS WSIGDENFNK IISFLYSTVG ALNKIGTDGT QVAMVQFTDD PRTEFKLNAY KTKETLLDAI KHISYKGGNT KTGKAIKYVR DTLFTAESGT RRGIPKVIVV ITDGRSQDDV NKISREMQLD GYSIFAIGVA DADYSELVSI GSKPSARHVF FVDDFDAFKK IEDELITFVC ETASATCPVV HKDGIDLAGF KMMEMFGLVE KDFSSVEGVS MEPGTFNVFP CYQLHKDALV SQPTRYLHPE GLPSDYTISF LFRILPDTPQ EPFALWEILN KNSDPLVGVI LDNGGKTLTY FNYDQSGDFQ TVTFEGPEIR KIFYGSFHKL HIVVSETLVK VVIDCKQVGE KAMNASANIT SDGVEVLGKM VRSRGPGGNS APFQLQMFDI VCSTSWANTD KCCELPGLRD DESCPDLPHS CSCSETNEVA LGPAGPPGGP GLRGPKGQQG EPGPKGPDGP RGEIGLPGPQ GPPGPQGPSG LSIQGMPGMP GEKGEKGDTG LPGPQGIPGG VGSPGRDGSP GQRGLPGKDG SSGPPGPPGP IGIPGTPGVP GITGSMGPQG ALGPPGVPGA KGERGERGDL QSQAMVRSVA RQVCEQLIQS HMARYTAILN QIPSHSSSIR TVQGPPGEPG RPGSPGAPGE QGPPGTPGFP GNAGVPGTPG ERGLTGIKGE KGNPGVGTQG PRGPPGPAGP SGESRPGSPG PPGSPGPRGP PGHLGVPGPQ GPSGQPGYCD PSSCSAYGVR APHPDQPEFT PVQDELEAME LWGPGV //