ID A0A8C9Q4S5_SPEDA Unreviewed; 1314 AA.
AC A0A8C9Q4S5;
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};
OS Spermophilus dauricus (Daurian ground squirrel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Spermophilus.
OX NCBI_TaxID=99837 {ECO:0000313|Ensembl:ENSSDAP00000018032.1, ECO:0000313|Proteomes:UP000694422};
RN [1] {ECO:0000313|Ensembl:ENSSDAP00000018032.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSDAP00000018032.1}
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; ENSSDAT00000020627.1; ENSSDAP00000018032.1; ENSSDAG00000016039.1.
DR Proteomes; UP000694422; 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: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 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:UP000694422};
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..1314
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034904330"
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 225..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..365
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1033
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1314 AA; 134352 MW; B5BD478DA8B853EF CRC64;
RNGQCWRVLL LLSISALLSA VTQTRASTEL ASQSHLDLTE LIGVPLPSSV SFVTGYSGFP
AYSFGPGANV GRPARTLIPP TFFRDFAVSV TVKPSSPSGG VLFAITDAFQ KVIYLGLRLS
GVEDGRQRVI LYYTEPGSHV SQEAAAFSVP VMTNRWSRFA VIVQGEAVTL LVDCEEHSHV
LFQRSSRPLA FEPSAGIFVG NAGATGLERF TGSIQQLIIH SDPRTPEELC EAQESSASGE
GSGLQDPDTV AEILEAVTHT QAPPEEAKVD PINIPPTSPS PYEDTELSGE PIPEETPENT
SSVVQHSNLE PGSGEILNDT LEGLPPVDGD PIPEIGSGSG AFPVTEEEGL AATAAGEAEV
SVSATPEAEL SSSPTGKSTL PMTTQDPGEG FTSDNEGLAM TATGEAEVPV STAGETEAGS
MPTGEPAFST FTQDSGEDTT LGPKDEEHLT TAVAASEVPL VTFEEEEASG VPTEGLVTLA
PTAAPGQMVT PAPGDDHWAA TSTEEPPATP GGEGPSSAPP DGPPLPVPTA APERQVTPPV
GVEAEGSGLG WGLDGGSGSG DLVGSEELLR GPPGPPGPPG LPGIPGKPGT DVFNGPPGSP
GKDGAAGEPG PPGPEGRPGP DGASGIPGMK GEKGARGPNG SVGEKGDPGS RGLPGPPGKN
GQVGTPGVRG PPGPPGPPGP PGPGCTTELG FEGPKGEKGD QGPKGERGMD GASTVGPPGP
RGPPGRIEIL SSSLINITRG SMNLSDIPEL MGPPGPDGLP GLPGFPGPRG PKGDTGVPGF
PGLKGEQGEK GEPGAILTGD TPLERLKGKK GEPGMHGTPG PMGPKGPPGH KGEFGLPGRP
GRPGLNGLKG AKGDRGIMMP GPPGLPGPPG PPGPPGAVVN IKGAVFPVPA RPHCKTPVGT
THPGDSELIT FHGVKGEKGS WGLPGSKGEK GDQGAQGPPG PPVDPVYLRH FLNSLKGENG
DRGFKGEKGD SHDNFFVPGP PGLPGNPGLV GQKGETVVGP QGPPGIPGLP GPPGFGRPGA
PGPPGPPGPP GPPAILGAAV ALPGPPGPPG QPGLPGSRNL VTAFSNMNDM LQKAHLVIEG
TFIYLRDSAE FFIRVRDGWK KLQLGELIPI PADSPPPPAL SSNPYQLQPP LNPILSANYE
NPALHLVALN MPFSGDIRAD FQCFQQARAA GLLSTFRAFL SSHLQDLSTV VRKAERYSLP
IVNLKGQVLF NNWDSIFSGQ GGQFNAHVPI YSFDGRDVMT DPSWPQKVVW HGSNTHGVRL
VDKYCEAWRT ADMAVTGFAS PLSTGKILDQ KAYSCANRLI VLCIENSFMT DARK
//
