COEA1_HUMAN
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 03-AUG-2022, entry version 177.
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
RC PNS {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 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. [Q05707-1]
DR RefSeq; XP_016869298.1; XM_017013809.1. [Q05707-1]
DR AlphaFoldDB; Q05707; -.
DR SMR; Q05707; -.
DR BioGRID; 113219; 82.
DR ComplexPortal; CPX-1755; Collagen type XIV trimer.
DR IntAct; Q05707; 34.
DR STRING; 9606.ENSP00000297848; -.
DR GlyConnect; 1132; 18 N-Linked glycans (4 sites).
DR GlyGen; Q05707; 19 sites, 17 N-linked glycans (4 sites), 8 O-linked glycans (7 sites).
DR iPTMnet; Q05707; -.
DR PhosphoSitePlus; Q05707; -.
DR BioMuta; COL14A1; -.
DR DMDM; 125987815; -.
DR EPD; Q05707; -.
DR jPOST; Q05707; -.
DR MassIVE; Q05707; -.
DR MaxQB; Q05707; -.
DR PaxDb; Q05707; -.
DR PeptideAtlas; Q05707; -.
DR PRIDE; Q05707; -.
DR ProteomicsDB; 58350; -. [Q05707-1]
DR ProteomicsDB; 58351; -. [Q05707-2]
DR ProteomicsDB; 58352; -. [Q05707-3]
DR Antibodypedia; 13712; 117 antibodies from 24 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 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; RITWDPA; -.
DR OrthoDB; 67372at2759; -.
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; 11 hits in 1070 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 167 other tissues.
DR ExpressionAtlas; Q05707; baseline and differential.
DR Genevisible; Q05707; HS.
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 CDD; cd00063; FN3; 8.
DR Gene3D; 2.60.40.10; -; 8.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF00041; fn3; 8.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF53300; SSF53300; 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 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
