ID A0A6J3ETK1_SAPAP Unreviewed; 1388 AA.
AC A0A6J3ETK1;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|RefSeq:XP_032096066.1};
OS Sapajus apella (Brown-capped capuchin) (Cebus apella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Sapajus.
OX NCBI_TaxID=9515 {ECO:0000313|Proteomes:UP000504640, ECO:0000313|RefSeq:XP_032096066.1};
RN [1] {ECO:0000313|RefSeq:XP_032096066.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_032096066.1};
RG RefSeq;
RL Submitted (AUG-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_032096066.1; XM_032240175.1.
DR GeneID; 116524752; -.
DR CTD; 1306; -.
DR Proteomes; UP000504640; Unplaced.
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 ECO:0000313|RefSeq:XP_032096066.1};
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:UP000504640};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1388
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026824700"
FT DOMAIN 40..228
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 89..227
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 229..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..420
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..530
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..605
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..731
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1388 AA; 141905 MW; 56FFC56DE3816493 CRC64;
MVPPRRNGQC WCLLVLLSVS APLPAVTQTR AATESASQGH LDLTQLIGVP LPSSVSFVTG
YGGFPAYSFG PGANVGRPAR TLIPSTFFRD FAISVTVKPS STRGGVLFAI TDAFQKVIYL
GLWLSGVEDG QQRIILYYTE LGSHVSQEVA AFSVPVMTHR WNRFAVIVQG EEVTLLVDCE
EHSRISFQRS SRPLAFESSA GIFVGNAGAT GLERFTGSIQ QLIVHPDPRT PEELCDAEES
SASGETSGLQ ETDGVAEILE AVTYTQAPPE EAKVEPINIP PTPSSLTEDM ELSGEPVPER
TPETTNMGIL QHSSPEQGSG DILNDTLEGV HSVDGDPITD SGSGAGAFLN ISEEKNLAAT
AAGLAEVAIS TAGETEAGSV PTGGPTLSMS TQNPEDGVTP GPDNEEVLAA TAAGEAKAPA
STPGEAEASG MPSGEPDLSV STQSLGEEAT VGPNSEESLT TATAAIEVPL STFEDEEASG
IPTDVLAPTT ATAGPEQAVT SGPGDEEDLA AATTAKPPTT AGGEESGSLP PDGPPLPLPT
VAPERWVTPA QREHVRMKEQ ARPKGEKGDA GEELPSPPEP SRPVGPTVGA EVEGSGLGWG
SGISSGSGDL VGSEELLRGP PGPPGPPGVP GIPGKPGTDV FMGPPGSPGE DGAAGEPGPP
GPEGQPGVDG ATGLPGMKGE KGARGPNGSV GEKGDPGNRG LPGPPGKQGQ AGPPGVMGPP
GPPGPPGPPG PGCAMGLGFE ETEGSGSTQL LNEPKLPRPT AAIGLKGEKG DRGPKGERGM
DGASIVGPPG PRGPPGRIET LSSSLINITH GFMNFSDIPE LVGPPGPDGL PGLPGFPGPR
GPKGDTGLPG FPGLKGEQGE KGEPGAILTG DVPLERLMGK KGEPGMHGAP GPMGPKGPPG
HKGEFGLPGR PGRPGLNGLK GAKGDPGVIM KGPPGLPGPP GPPGPPGAVI NIKGAVFPIP
VRPHCKIPVG TAHPGSPELI TFHGVKGEKG SWGLPGSKGE KGDQGAQGPP GPPLDLTYLR
HFLNNLKGEN GDKGFKGEKG EKGEFNGSFL MSGPPGLPGN PGMAGQKGET VIGPQGPPGA
PGLPGPPGFG RPGDPGPPGP PGPPGPPAIL GAAVALPGPP GPPGQPGLPG SRNLVTAFSN
MDDMLQTAHL IIEGTFVYLR DSTEFFIRVR DGWKKLQLGE LIPIPADSPP PPALSSNPHQ
PLPPLNPISS ANYERPALHL AALNMPFSGD IRADFQCFKQ ARAAGLLSTY RAFLSSHLQD
LSTIVRKAER YSLPIVNLKG QVLFNNWDSI FSGHGGQFNT HNPIYSFDGR DIMTDPSWPQ
KVIWHGSSPH GVRLVDNYCE AWRTADTAVT GFASPLSTGK ILDQKAYSCA NRLIVLCIEN
SFMTDARK
//
