ID A0A2K6EL47_PROCO Unreviewed; 1386 AA.
AC A0A2K6EL47;
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};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSPCOP00000002452.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000002452.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000002452.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPCOP00000002452.1}
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 RefSeq; XP_012493757.1; XM_012638303.1.
DR STRING; 379532.ENSPCOP00000002452; -.
DR Ensembl; ENSPCOT00000008464.1; ENSPCOP00000002452.1; ENSPCOG00000007449.1.
DR GeneID; 105805409; -.
DR KEGG; pcoq:105805409; -.
DR CTD; 1306; -.
DR GeneTree; ENSGT00940000158302; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000233160; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
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: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 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 Pfam; PF13385; Laminin_G_3; 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:UP000233160};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1386
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014369082"
FT DOMAIN 39..227
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 88..226
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 230..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..541
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..921
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..947
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 140625 MW; 418417539C584FA2 CRC64;
MAPRRNGRHW CLMLLLSVSA LLSAVTQIRA ATEPASQGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPVRT LIPSTFFRDF AISVTVKPSS AHGGVLFAIT DAFQKVIYLG
LRLSGVEDGH QRVILYYTEP GSHVSHEAAA FSVPVMTNRW NRFAVIVQDE EVTLLVDCEE
HSHVAFQRSP RALAFEPSAG IFVGNAGATG LERFTGSIQQ LTVYPDPRTP EELCEAEESS
ASGEASGLQE TAGVAETVEA VTYTQAPPQE AKVEPINTPP TPPSPPEDTE LSGEPVPEGT
PETTNVSVVQ HSSPEEGSGQ MLNDTLEGVH AVDGDPITDT GSGSGDGASL DIIEEKGLAT
TAAGPAEVPI STAGEAEADS VPTGGPTLSM ATQKPGEGVT PGLDDEEGSA ATAAEEAEVP
TSTAGETEPG SVPTGGLALL QATQPPSEEV TPGPNGEESS TTAAAVTELL LSTSEDEEAS
GVPTDGLGPL TPTAAPGQAV TSGPGDEDGL ATATTEEPLT MAGGEEPGSA PPDGPPLPVP
TAAPERAVTL AQTVHAGMKE QAVPKGETGD AGEGLPGSPE PSAPARPTVG AEVEGSGPVW
GLDVGSGSGD QMGSEELLRG PPGPPGPPGS PGIPGKPGTD VFTGPPGSPG EDGAAGEPGP
PGPKGQPGVD GVTGLPGMKG EKGARGPNGS VGEKGDPGNR GLPGPPGKNG QVGTPGIMGP
PGPPGPPGPP GPGCAMGLGF EDTEGSGSIS LLHEPRISGP VVPSGPKGEK GERGPKGDRG
MDGASIVGPP GPRGPPGRVE FLSSSLINIT HGSMNLSGIP ELVGPPGPDG TPGLPGFPGP
RGPKGDTGVP GFPGLKGEQG EKGEPGAILT GDVPLERLMG KKGEPGVHGA PGPMGPKGPP
GHKGELGLPG RPGRPGLNGP KGAKGDRGVM MPGPPGLPGP PGPPGPPGAV INIKGAVFPI
PVRPHCKTPV GTTHPGNPEL ITFHGVKGEK GSWGLPGTKG EKGDQGAQGP PGPPVDPAYL
RHFLNSLKGE NGDRGFKGEK GDSNDNFFVS GPPGLPGNPG LAGQKGETVI GPQGPPGVPG
LPGPPGFGRP GAPGPPGPPG PPGPPAILGA AVALPGPPGP PGQPGLPGSR NLVTTFSNMD
DMLQKAHLVI EGTFIYLRDS TEFFIRVRDG WKKLQLGELI PLPADIPPPP ALSSNPHHPQ
PPLNPHSSAN YEKPALHLVA LNMPFSGDIR ADFQCFQQAR AAGLLSTYRA FLSSHLQDLS
TVVRKAERHS LPIVNLKGQV LFNNWDSIFA GHGGQFNTHI PIYSFDGRDV MTDPSWPQKV
IWHGSSPHGV RLVDKYCEAW RTGDMAVTGL ASPLSSGKIL DQKTYSCANR LIVLCIENSF
MTDARK
//
