ID A0AA97K156_EUBMA Unreviewed; 1288 AA.
AC A0AA97K156;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|RefSeq:XP_054846884.1};
OS Eublepharis macularius (Leopard gecko) (Cyrtodactylus macularius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Gekkota; Eublepharidae; Eublepharinae;
OC Eublepharis.
OX NCBI_TaxID=481883 {ECO:0000313|Proteomes:UP001190640, ECO:0000313|RefSeq:XP_054846884.1};
RN [1] {ECO:0000313|RefSeq:XP_054846884.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_054846884.1};
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_054846884.1; XM_054990909.1.
DR GeneID; 129337303; -.
DR CTD; 1306; -.
DR Proteomes; UP001190640; Chromosome 11.
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; 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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 5.
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 ECO:0000313|RefSeq:XP_054846884.1};
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:UP001190640};
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..1288
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041712436"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 87..225
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 224..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..411
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..530
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..633
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..749
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..827
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..964
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1007
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1025
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1288 AA; 132467 MW; D3B1117386AC28C2 CRC64;
MPPSHSRRPW NLCLLLLGSL LPAVLPAQVI EERGSKGHLD LTELIGVPLP PSVSFITGYG
GFPAYSFGPD ANIGRLTRTL LPPQFFRDFA VAVTVKPNSD RGGVLFAITD AFQKTIYLGV
RLSPVDDGTQ RIIMYYTEPG SHISREAASF KVPVMTNKWN RFTITVQEND IVLFMDCEEY
HRIQFQRFAQ TLFFEPSSGI FVGNAGATGL ERFTGSIQQL TIKTDPKAAE EQCEDDDSYG
SGESSGHDDI QEQEGIPETQ EVIWPTPTKL PQLVGNQSEE TTSRPVGAPP TLSTNSEEVD
FSGQHLWEAS VAPTEVKDQG VTTTETTQKE TETTTVAPEV LETEAGPHNR VLQGTPLEKG
QKGEKGQKGE EGPPGPPGRA GPNATWPETP GPPGPPGKPG LDGKPGIPGK DGLMGEPGAH
GSPGQKGDPG PKGEKGDVAV GSPGLPGLPG PPGPPATSRK RIEMEGSGSG DFDKDIELPR
GAPGPPGPPG PPGEPGLPGP DSDAGVPGLP GRNGKDGDPG QPGPQGPPGH PGQDGLVSLK
GSKGEKGDQG LPGAAGPKGD PGDVGSPGQK GQPGADGEPG KPGLPGLPGP PGPGYGFGFE
DMEGSGIVGS SSGPAILGSS GPVGPAGGTG VRGPMGPKGE TGDVGLPGLT GIKGEQGLEG
KPGFPGVAGR PGDAGSKGEK GDPGPKGEPG EPGVSVVGPP GPPGPPGPII AIPRSLNTSD
ESFNITALQG LGPPGPDGKP GLPGFPGPKG PKGDIGLPGL PGEKGKQGEK GEPGVIFAST
DSVTELIRRP GEKGEPGEMG PRGPMGPIGP IGPKGELGFP GRPGRPGLNG LRGIKGERGV
TLYGHPGTPG PPGPPGPPGR VVYIKGTVFP VSPRPHCKTP VTTAHSGDQA ATDSSWGVQG
PLGVKGEKGD RGLPGPPLPS TYFSHFKGEK GNNGENGLKG EKGEPNGEFF MSGPPGLPGR
PGPVGPKGDT VVGPRGPPGV PGLPGPPGFG PVGPPGPPGP PGPPGPPSIY GSAAVPGPPG
PPGEPGLPGA RNLVTTLRNV DTMLQKVHLV SEGTLIYLSE TSEIFLRVQD GWKKLQLGDL
IPIPADSPPP PAISSPDFQP LPAPFPASSA DRGRPSLHLV ALNTPFSGDM RADYQCFQQA
RAAGLFSTYR ALLSSHLQDL LTVVRKVDRY HLPIVNLKGE TLFNNWESIF SGNGGQFDTR
IPIYSFDGRN VMTDPAWPQK VVWHGSSPHG IRLVSSYCEA WRTADVAVMG QASPLKSGKL
LDQKAYSCSN RFIVLCIENS YISDDQRK
//
