ID A0A8C2VZU9_CHILA Unreviewed; 1399 AA.
AC A0A8C2VZU9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSCLAP00000020099.1};
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:ENSCLAP00000020099.1, ECO:0000313|Proteomes:UP000694398};
RN [1] {ECO:0000313|Ensembl:ENSCLAP00000020099.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCLAP00000020099.1}
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; ENSCLAT00000020292.1; ENSCLAP00000020099.1; ENSCLAG00000013771.1.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000694398; 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:0005783; C:endoplasmic reticulum; IEA:Ensembl.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF714; COLLAGEN ALPHA-4(IV) CHAIN; 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}.
FT DOMAIN 63..251
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 112..250
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..644
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..671
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..745
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..934
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..960
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1399 AA; 143563 MW; 9D382E20B846F061 CRC64;
MAPRWDPLPS PRGPPTHPTS RLTCSPSTPS CSNWRLRLLL STSALLSAVS GTRASTDSAS
QGHLDLTQLI GVPLPSSVSF VTGYGGFPAY SFGPGANIGR PARTLIPPTF FRDFAISVMV
KPSSTRGGVL FAITDAFQKV IYLGLRLSGV EDGHQRVILY YTEPGSHVSH EAAVFSVPVM
ANRWNHFAVI VQGEEVTLLM DCEEHSQALF QRSSRPLAFD PSTGIFVGSA GATGLDRFTG
ALQQLTIHAD PRTPEELCEA QESSASGEAS GLQESEAETV AEILEAVTYT QAPAKEAKVE
PINTPPTSFS PLEDTELSGE PVPEGTPETN LSISQHNSPE QGSGEILNDT LERVHTVDGD
AIADAGSGER AFLDATEEQG SAATVAGEDE VTTSTPQEAE VSSMPAAAPT LAVSTLNPQE
GTTPDLEDEE GSAAMGTGEA KAPVSTAGEV ESGSLPTVGP TFTMSTQSPR EETTLGPGEE
WLTTATATTE VSLSTFGEEE ASGASTDDLT VLTPTVAPAH AGGPSTDDLA VLTPTAALGQ
VVTPAPDDME DLEPLATAGG EGISSAPPAG LPLPVPTVAP ERRVTLAHLL HGEVEGPEGE
KVGAEAEGSD PGWGLDIGSG SGDLVDREEL LRGPPGPPGP PGLPGIPGKP GTDVLMGPPG
SPGEDGAAGE PGLPGPEGEP GLDGATGRPG IKGEKGARGP NGSVGEKGDP GNRGLPGPPG
KNGQAGTPGI MGPPGPPGPP GPPGPGCATG PEFEDTEGSG NIRLLSEPRI SRPTVSTGLK
GEKGDQGPKG ERGLDGVSTV GPPGPRGPPG RIEILSSSLI NITHGSLNFS DIPELLGPPG
PDGLPGLPGF PGPRGPKGDT GLPGFPGLKG EQGEKGEPGT ILTGDVPLER LKGRKGEPGL
HGAPGPMGPK GPPGHKGEFG LPGRPGRPGL NGLKGAKGDR GIMMPGPPGQ PGPPGPPGPP
GAVINIKGAV FPVPVRPHCK MPVGTAHPGD PELITFHGVK GEKGSWGLPG SKGEKGDQGA
QGPPGPPVDP VYLRHFLNSL KGENGDRGFK GEKGDSNENF FVSGSPGLPG NPGLAGQKGE
AIMGPQGPPG IPGLPGPPGF GRPGAPGPPG PPGPPGPPAI LGAAVALPGP PGPPGQPGLP
GSRNLVTAFS SMDDMLQKAH LVIEGTFIYL RDSTEFFIRV RDGWKKLQLG ELIPIPADSP
PPPALSSNSY QLQPPLNPIL SGNYESPALH LVALNMPFSG DIRADFQCFQ QARAAGLLST
FRAFLSSHLQ DLSTVVRKAE RYSLPIVNLK GQVLFNNWDS IFSGDGGQFN THVPIYSFDG
RDVMTDPSWP QKVIWHGSTT HGVRLVDKYC EAWRTADMAV TGFASPLSTG KILDQTPYSC
ANRLIVLCIE NSFMTDARK
//
