ID A0A6P6DMQ4_OCTDE Unreviewed; 1397 AA.
AC A0A6P6DMQ4;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=Col15a1 {ECO:0000313|RefSeq:XP_023561221.1};
OS Octodon degus (Degu) (Sciurus degus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Octodontidae;
OC Octodon.
OX NCBI_TaxID=10160 {ECO:0000313|Proteomes:UP000515203, ECO:0000313|RefSeq:XP_023561221.1};
RN [1] {ECO:0000313|RefSeq:XP_023561221.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-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_023561221.1; XM_023705453.1.
DR FunCoup; A0A6P6DMQ4; 255.
DR GeneID; 101585954; -.
DR CTD; 1306; -.
DR InParanoid; A0A6P6DMQ4; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000515203; 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 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; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1106; VIKING, ISOFORM A; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 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 ECO:0000313|RefSeq:XP_023561221.1};
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:UP000515203};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1397
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028339973"
FT DOMAIN 62..250
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 256..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..642
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..669
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1397 AA; 143286 MW; E32DB28C9D04B855 CRC64;
MAPRSSWRLR LLLSTSALLS TVTGTLASTG LVLSTVLRHI PHIGSAMQEG KWPDQDSASQ
GHLDLTQLIG VPLPSSVSFV TGYGGFPAYS FGPGANIGRP ARTLIPPTFF RDFAISVLAK
PSSTQGGVLF AITDAFQKVI YLGLRLSDVE DGHQRVILYY TEPGSHVSHE AAVFLVPVMT
NRWMHFAVIV QGEEVTLLMD CEEHSHVLFQ RSSGPLAFEP STGIFVGSAG ATGLDRFTGS
IQQLTIHADP RMPEELCEAQ ESSASGEASG LQETDTETVA EILEAITYTQ APPKEAKPEP
INIPPTSSSA LEDMELSGEP VMEGTLETNL SISQHSSPEQ GSGEVLNDTL ERVPAVDGDA
VADAGSGERA FPDTTEEQSP AATAAGEDLV TTSTNQEAEG SSIPTAVPTL AMSTLAPQEG
TIPGLEDEEG SAAMGTGEAE MPVNTAGEVE SGSMPTEGPS FTVSTWSPRE ETTLGPDEAL
SIMATAATAV PLGPFEEEAA SGAFTDDQAI LTPTVAPVQA SGASTDDLAV LTSTVALGQV
VTPTPEDEDL EPLATAGGDG VSSAPPAGLP LPEPTAAPER RVTLAQLVHG EMEEPTGVKV
AAEAEGSGQG WSLDIGSGSG DLVDREELLR GPPGPPGPPG SPGLPGKPGA DVLMGPPGSP
GEDGAAGEPG LPGPEGEPGL DGAIGRPGIK GEKGARGPNG SVGEKGDPGN RGLPGPPGKN
GQAGTPGVMG PPGPPGPPGP PGPGCATGLE SEDTEGSGHI PLLREPGISR PTVSSGLKGE
KGDQGPKGER GLDGTSTVGP PGPRGPPGRI EILSSSLINI THGSLNFSDI PELLGPPGPD
GLPGLPGFPG PRGPKGDTGL PGFPGLKGEQ GEKGEPGAIL TGDVPLERLK GTKGEPGLHG
APGPMGPKGP PGHKGEFGLP GRPGRPGLNG LKGAKGDRGI MMPGPPGLPG PPGPPGPPGA
VVNIKGAVFP VPVRPHCKMP VGTTQPGDPE LITFHGVKGE KGSWGLPGSK GEKGDQGAQG
PPGPPVDPAY LRYFLNSLKG ENGDRGFKGE KGDSNDNFFV SGSPGLPGNP GVAGQKGEAI
VGPQGPPGIP GQPGPPGFGR PGAPGPPGPP GPPGPPAILG AAVALPGPPG PPGQPGLPGS
RNLVTAFSNM DDMLQKAHLV IEGTFIYLRD STEFFIRVRD GWKKLQLGEL IPIPADSPPP
PALSSNSYQL QPPLNPILSG NYENPALHLI ALNMPFSGDI RADFQCFQQA RAAGLLSTFR
AFLSSHLQDL STVVRKAERY SLPIVNLKGQ VLFNNWDSIF SGDGGQFNTQ VPIYSFDGRD
VMTDPSWPQK VVWHGSTPHG VRLVDKYCEA WRTADMAVTG FASPLSTGKI LEQKPYSCAN
RLIVLCIENS FMTDARK
//
