ID A0A2K5K5Y4_COLAP Unreviewed; 1374 AA.
AC A0A2K5K5Y4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 39.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000036511.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000036511.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCANP00000036511.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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}.
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DR Ensembl; ENSCANT00000059760.1; ENSCANP00000036511.1; ENSCANG00000041935.1.
DR OMA; RATEDQC; -.
DR Proteomes; UP000233080; 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:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-ARBA.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR CDD; cd00110; LamG; 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; 3.
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};
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:UP000233080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 26..214
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 75..213
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 209..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..458
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..526
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..717
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1093
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1374 AA; 140168 MW; 6FD5C8CCECA4189B CRC64;
MLLSVSTPLP AVTQTRAATE SASQGHLDLT QLIGVPLPSS VSFVTGYGGF PAYSFGPGAN
VGRPARTLIP STFFRDFAIS VMVKPSSTHG GVLFAITDAF QKVIYLGLRL SGVEDGHQRV
ILYYTEPGSH VSQEAAAFSV PVMTHRWNRF AVIVQGEEVA LLVDCEEHSR IPFQRSPQAL
TFESSAGIFV GNAGATGLER FTGSLQQLTV HPDPRTPEEL CDPEESSASG ETSGLQEADG
VAEILEAVTY TQAPPKEAKV EPINTPPTPS SPFEDMELSG EPVPEGTPET TNMSIIQHSS
PEQGKGAILN DTLEGIHSVD GDPITDSGSG AGAFLDIAEE KNLAATAVGL AEAPISTAGE
AEASSVPTGG PTLSVSTQNP EEGVTPGPDN EESLAATAAG EAEALASTPW EAEASGVPPG
EPDLSMSPQS LGEEATVGPS SEESLTTAAA ATEVSLSTFE DEEASGVPTD GLAPLTATMT
PEQAVTSGPG DEEDLAAATT EEPLITARGE ESGSPPPDGP PLPLPTVAPE RRVTPAQREH
VGMKGQAEPK GEKGDAGEEI PGPPEPSGPV GPTVGAEAEG SGLGWGSDVG SGSGDLVGSE
ELLRGPPGPP GPPGLPGIPG KPGTDVFLGP PGSPGEDGRA GEPGPPGPEG QPGVDGATGL
PGMKGEKGAR GPNGSVGEKG DPGNRGLPGP PGKKGQAGPP GVMGPPGPPG PPGPPGPGCT
MGLGFEDTEG SGSTQLLSEP KLSRPTAAIG PKGEKGDQGP KGERGTDGAS IVGPPGPRGP
PGRIEVLSSS LINITHGFMN FSDIPELVGP PGPDGLPGLP GFPGPRGPKG DTGLPGFPGL
KGEQGEKGEP GAILTGDIPL ERLMGKKGEP GMHGAPGPMG PKGPPGHKGE FGLPGRPGRP
GLNGLKGAKG DPGVIMQGPP GLPGPPGLPG PPGAVINIKG AIFPIPVRPH CKMPVGTAHP
GSPELITFHG VKGEKGSWGL PGSKGEKGDQ GAQGPPGPPL DLAYLRHFLN NLKGENGDKG
FKGEKGEKGD INDGFLMSGP PGLPGNPGLA GQKGETVIGP QGPPGAPGLP GPPGFGRPGD
PGPPGPPGPP GPPAILGAAV ALPGPPGPPG QPGLPGSRNL VTAFSNMDDM LQKAHLVIEG
TFIYLRDSTE FFIRVRDGWK KLQLGELIPI PADSPPPPAL SSNPHQLLPP PNPISSTNYE
KPALHLAALN MPFSGDIRAD FQCFKQARAA GLLSTYRAFL SSHLQDLSTI VRKAERYSLP
IVNLKGQVLF DNWDSIFSGH GGQFNMHIPI YSFDGRDIMT DPSWPQKVIW HGSSPHGVRL
VDNYCEAWRT TDTAVTGLAS PLRTGKILDQ KAYSCANRLI VLCIENSFMT DARK
//
