ID A0A2I0M4W9_COLLI Unreviewed; 1263 AA.
AC A0A2I0M4W9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|EMBL:PKK24724.1};
GN ORFNames=A306_00011017 {ECO:0000313|EMBL:PKK24724.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Columbimorphae; Columbiformes;
OC Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK24724.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK24724.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK24724.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- FUNCTION: Restin potently inhibits angiogenesis.
CC {ECO:0000256|ARBA:ARBA00058706}.
CC -!- FUNCTION: Structural protein that stabilizes microvessels and muscle
CC cells, both in heart and in skeletal muscle.
CC {ECO:0000256|ARBA:ARBA00058695}.
CC -!- SUBUNIT: Interacts moderately with EFEMP2.
CC {ECO:0000256|ARBA:ARBA00065596}.
CC -!- SUBUNIT: Trimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00061770}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK24724.1}.
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DR EMBL; AKCR02000040; PKK24724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0M4W9; -.
DR GeneID; 102095712; -.
DR CTD; 1306; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.40.1620.70:FF:000002; Collagen alpha 1 (XV) chain; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:PKK24724.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1263
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014143053"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 87..225
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 225..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..423
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..469
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..527
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..587
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..610
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..658
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..728
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..783
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..794
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..893
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..983
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1006
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 130167 MW; E08131421A5A870A CRC64;
MLSRHAWWTW DLLLLLFGLL IYDGSAAEII EERGSKGHLD LMELIGVPLP PSVYFVTGYG
GFPAYSFGPD ANIGRLTRAI IPSPFYRDFT IVVTMKPNSD HGGVLFAITD ALQKTIYLGM
RLSPVDDSTQ RIIMYYTEPG SQISREAASF KVPVMTNRWN RFTATVQGND VALFMDCEEY
QRVQFQRSGQ ALVFESGSGI FVGNAGATGL EKFTGSIQHL TIKSDPRAAE DHCEDDDSYV
SGDNSGNGSI QDHEGISETQ EVLAPSYLPI RPGDTLAEPV EAPAAVLSYL EENDSSGNHR
SEETSEGAKP KEQESAVMKT EQSNRESTTV VQTISREEDG SGATVLPGVS REEGQKGQEG
EDEPTGSPRM PEVEDTQKKD QGPPGPPGKL GQHGQPGVPG KNGLPGKDGP QGLPGLKGKA
GLKGVKGDPG EGLPGPPGLP GPGGPSAPSR GLNRPEPEES GSGDIDGETE ILRGLPGPPG
LPGLPGKPAP DSGVGPPGSP GEDGASGEQG PEGPQGPPGL DGVVGPPGRK GEKGDRGLPG
TVGPRGDPGV TGSRGPKGEA GAVGSPGKPG PTGPPGSPGP PGPPGPPGLS YSLGFEDMEG
SGSIGLLSES RVPGSRRSKG SAERQGQRGP LGPKGPKGEK GDQGPQGEPG QDGNSIVGPP
GPPGPPGPII AIPELLLNNT DGNFNFTGIK GLLGPPGLDG KPGLPGFPGP RGPKGDTGLP
GLQGPKGQQG EKGEPGAIIS ADGSLTELLG RKGEKGEAGA VGPVGPMGPI GPTGPKGGLG
FPGRPGRPGL NGLRGVKGDR GEPFNGLPGL PGPPGPPGPP GRIVYIKGTV FPVSPRPHCK
MPVSTPCPGN QGTLSVHGAK ANRGSWGLHS SADLKGEKGD RGAPGPPGSP LPPSYFSHLI
NSIKGEKGDN GVSGVKGEKG EPNGGFFLTG PPGPAGRPGL VGPKGDSVVG PRGPPGLPGL
PGLPGYGKIG PPGPPGPPGP PGPTAIYGSA AAMPGPPGPP GEPGPPATRN LVTTFQNIEG
MLEKVHLVAE GTLIYLSETS EVFIRIRNGW RKLQLGELIL VPADSLPPPA ISSHSLPALS
PISNMNNGKP ALHLVALNLP FSGDVRADFQ CFQQAQLAGL TSTYRAFLSS HLQDLATIVR
KTDRYHLPIV NLKGETLFNN WESIFNGNGG QFNIHVPIYS FDGRNVMTDP AWPQKIIWHG
STANGIRLVS SYCEAWHTAD MRELGQASQL KTGKLLDQKV YSCSNQFIVL CIENSFVSEP
QGK
//
