ID A0A8C3WQW8_9CETA Unreviewed; 1340 AA.
AC A0A8C3WQW8;
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:ENSCWAP00000019962.1};
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:ENSCWAP00000019962.1, ECO:0000313|Proteomes:UP000694540};
RN [1] {ECO:0000313|Ensembl:ENSCWAP00000019962.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCWAP00000019962.1}
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; ENSCWAT00000021654.1; ENSCWAP00000019962.1; ENSCWAG00000015170.1.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000694540; Unplaced.
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 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..1340
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034108545"
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..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1082
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 561..585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..795
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..875
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..896
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1016
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1078
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1340 AA; 136327 MW; 80A625C00B604F73 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 GPTGPPGPPG PPGLPGIPGS PGTDVFVGPP
GSPGEDGPAG EPGPPGPEGK PGLDGASGLP GMKGEKGARG PNGSVGEKGD PGSRGLPGPP
GKNGQVGTPG VMGPPGPPGP PGPPGPGCAT GLGFEDTEGS GSIRLLHEPG ISGPVASAGP
KGEKGDQGPK GDRGMDGASI VGPPGPRGPP GRIEVLSSSL INITHGFMNL SDIPELVGPP
GPEGIPGLPG FPGPRGPKGD TGVPGFPGLK GEQGEKGEPG AILTGDVPLE RLRGKKGEPG
EHGAPGPMGP KGPPGHKGEF GLPGRPGRPG LNGLKGAKGD RGVMMPGPPG LPGPPGPPGP
PGAVINIKGA VFPIPVRPHC KTPVGTTHPG NSELITFHGV KGEKGSWGLP GSKGEKGDQG
AQGPPGPPVD PAYLRHFLNS FKGENGDRGV KGEKGDAYGG FSVSGPPGLP GSPGLVGQKG
ETVIGPQGPP GAPGLPGPPG FGRPGSPGPP GPPGPPGPPA ILGAAVALPG PPGPPGQPGL
PGSRNLVTAF SNMDDMLQKA HLVIEGTFIY LRDSTEFFIR VRDGWKKLQL GELIPLPADS
LPPPALSGNP HQPQLPLTSI SSVNYGRPAL HLVALNTPFS GDLRADFQCF QQARAAGLLS
TYRAFLSSHL QDLSTVVRKA ERYSLPIVNL KGQVLFNNWD SIFSGHGGQF NTHVPIYSFD
GRDVMTDPSW PQKVVWHGSS THGVRLVDQY CEAWRTADVA VMGLASPLST GKILDQKAYS
CADRLIVLCI ENSFMTDARK
//
