ID A0A8C3WUJ5_9CETA Unreviewed; 1371 AA.
AC A0A8C3WUJ5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSCWAP00000019809.1};
OS Catagonus wagneri (Chacoan peccary).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Tayassuidae; Catagonus.
OX NCBI_TaxID=51154 {ECO:0000313|Ensembl:ENSCWAP00000019809.1, ECO:0000313|Proteomes:UP000694540};
RN [1] {ECO:0000313|Ensembl:ENSCWAP00000019809.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCWAP00000019809.1}
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; ENSCWAT00000021493.1; ENSCWAP00000019809.1; ENSCWAG00000015170.1.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000694540; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
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 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:UP000694540};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1371
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034235710"
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 224..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..477
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..580
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..593
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 703..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 859..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..906
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..928
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1047
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1090
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 139369 MW; 142104E5B258AEA0 CRC64;
MASRRDAQCW RLLLLLSISS LLPAVTRTRS ATELASQGHL DLTQLIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPAFFRDF AISVTVRPSS ARGGVLFAVT DAFQKVIYLG
LRLSAVEEGN QRVILYYTEP GSQVSREAAA FPVPVMTHRW NRFAVVVQGE EVSLLVECEE
QGHVSFPRSS QALAFEPSAG IFVGNAGATG LERFTGSIQQ LTIHADPRTP EELCEAEESS
ASGEASGLQE TDGVAETVEA ITYTQAPSEP AEVEPINTPP TPSPPSEDSE LSGKPVPEGT
QETANRSAFP HSSPEQGSGE ILSDTLERAH GVDGAPVTDT GSGEGALLHV FEESPHTEEG
LAATAAAGEA EMTISTSGEA EADSVPTEGP TLFMSAKDPG EEVTLGPDNE EGSAVTAAEE
AEVLISSTGE AEASSVPTGG PTLSVSTQDP GEGVTLGPIS EESLTTTAET AEAPLSTFEE
EEASRVPTDG LAPLTPTVAP KQAFTSGPGD EDLVAATAEE PLISSGAEEL GGVPPEGPPL
PIPTVAPERG TAPGEDEEGL PGPPPPTGPA GPTAGAEAEG SGLGWGLDIG SGSGDLVRSE
ELLRGPPGPP GPPGLPGIPG SPGTDVFVGP PGSPGEDGPA GEPGPPGPEG KPGLDGASGL
PGMKGEKGAR GPNGSVGEKG DPGSRGLPGP PGKNGQVGTP GVMGPPGPPG PPGPPGPGCA
TGLGFEDTEG SGSIRLLHEP GISGPVASAG PKGEKGDQGP KGDRGMDGAS IVGPPGPRGP
PGRIEVLSSS LINITHGFMN LSDIPELVGP PGPEGIPGLP GFPGPRGPKG DTGVPGFPGL
KGEQGEKGEP GAILTGDVPL ERLRGKKGEP GEHGAPGPMG PKGPPGHKGE FGLPGRPGRP
GLNGLKGAKG DRGVMMPGPP GLPGPPGPPG PPGAVINIKG AVFPIPVRPH CKTPVGTTHP
GNSELITFHG VKGEKGSWGL PGSKGEKGDQ GAQGPPGPPV DPAYLRHFLN SFKGENGDRG
VKGEKGDAYG GFSVSGPPGL PGSPGLVGQK GETVIGPQGP PGAPGLPGPP GFGRPGSPGP
PGPPGPPGPP AILGAAVALP GPPGPPGQPG LPGSRNLVTA FSNMDDMLQK AHLVIEGTFI
YLRDSTEFFI RVRDGWKKLQ LGELIPLPAD SLPPPALSGN PHQPQLPLTS ISSVNYGRPA
LHLVALNTPF SGDLRADFQC FQQARAAGLL STYRAFLSSH LQDLSTVVRK AERYSLPIVN
LKGQVLFNNW DSIFSGHGGQ FNTHVPIYSF DGRDVMTDPS WPQKVVWHGS STHGVRLVDQ
YCEAWRTADV AVMGLASPLS TGKILDQKAY SCADRLIVLC IENSFMTDAR K
//
