ID A0A8C2VVD5_CHILA Unreviewed; 1371 AA.
AC A0A8C2VVD5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSCLAP00000020100.1};
OS Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC Chinchillidae; Chinchilla.
OX NCBI_TaxID=34839 {ECO:0000313|Ensembl:ENSCLAP00000020100.1, ECO:0000313|Proteomes:UP000694398};
RN [1] {ECO:0000313|Ensembl:ENSCLAP00000020100.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCLAP00000020100.1}
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_005382882.1; XM_005382825.2.
DR Ensembl; ENSCLAT00000020293.1; ENSCLAP00000020100.1; ENSCLAG00000013771.1.
DR GeneID; 102017022; -.
DR CTD; 1306; -.
DR GeneTree; ENSGT00940000158302; -.
DR OMA; RATEDQC; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000694398; 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: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:UP000694398};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1371
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034036899"
FT DOMAIN 35..223
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 84..222
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..576
FT /note="Basic and acidic 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 634..643
FT /note="Low complexity"
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 893..906
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..932
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1090
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 140549 MW; 7BD06859102809C5 CRC64;
MAPSNWRLRL LLSTSALLSA VSGTRASTDS ASQGHLDLTQ LIGVPLPSSV SFVTGYGGFP
AYSFGPGANI GRPARTLIPP TFFRDFAISV MVKPSSTRGG VLFAITDAFQ KVIYLGLRLS
GVEDGHQRVI LYYTEPGSHV SHEAAVFSVP VMANRWNHFA VIVQGEEVTL LMDCEEHSQA
LFQRSSRPLA FDPSTGIFVG SAGATGLDRF TGALQQLTIH ADPRTPEELC EAQESSASGE
ASGLQESEAE TVAEILEAVT YTQAPAKEAK VEPINTPPTS FSPLEDTELS GEPVPEGTPE
TNLSISQHNS PEQGSGEILN DTLERVHTVD GDAIADAGSG ERAFLDATEE QGSAATVAGE
DEVTTSTPQE AEVSSMPAAA PTLAVSTLNP QEGTTPDLED EEGSAAMGTG EAKAPVSTAG
EVESGSLPTV GPTFTMSTQS PREETTLGPG EEWLTTATAT TEVSLSTFGE EEASGASTDD
LTVLTPTVAP AHAGGPSTDD LAVLTPTAAL GQVVTPAPDD MEDLEPLATA GGEGISSAPP
AGLPLPVPTV APERRVTLAH LLHGEVEGPE GEKVGAEAEG SDPGWGLDIG SGSGDLVDRE
ELLRGPPGPP GPPGLPGIPG KPGTDVLMGP PGSPGEDGAA GEPGLPGPEG EPGLDGATGR
PGIKGEKGAR GPNGSVGEKG DPGNRGLPGP PGKNGQAGTP GIMGPPGPPG PPGPPGPGCA
TGPEFEDTEG SGNIRLLSEP RISRPTVSTG LKGEKGDQGP KGERGLDGVS TVGPPGPRGP
PGRIEILSSS LINITHGSLN FSDIPELLGP PGPDGLPGLP GFPGPRGPKG DTGLPGFPGL
KGEQGEKGEP GTILTGDVPL ERLKGRKGEP GLHGAPGPMG PKGPPGHKGE FGLPGRPGRP
GLNGLKGAKG DRGIMMPGPP GQPGPPGPPG PPGAVINIKG AVFPVPVRPH CKMPVGTAHP
GDPELITFHG VKGEKGSWGL PGSKGEKGDQ GAQGPPGPPV DPVYLRHFLN SLKGENGDRG
FKGEKGDSNE NFFVSGSPGL PGNPGLAGQK GEAIMGPQGP PGIPGLPGPP GFGRPGAPGP
PGPPGPPGPP AILGAAVALP GPPGPPGQPG LPGSRNLVTA FSSMDDMLQK AHLVIEGTFI
YLRDSTEFFI RVRDGWKKLQ LGELIPIPAD SPPPPALSSN SYQLQPPLNP ILSGNYESPA
LHLVALNMPF SGDIRADFQC FQQARAAGLL STFRAFLSSH LQDLSTVVRK AERYSLPIVN
LKGQVLFNNW DSIFSGDGGQ FNTHVPIYSF DGRDVMTDPS WPQKVIWHGS TTHGVRLVDK
YCEAWRTADM AVTGFASPLS TGKILDQTPY SCANRLIVLC IENSFMTDAR K
//
