ID A0A1U7RJ56_ALLSI Unreviewed; 1303 AA.
AC A0A1U7RJ56;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 28-JAN-2026, entry version 39.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|RefSeq:XP_006019028.1,
GN ECO:0000313|RefSeq:XP_025054095.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006019028.1};
RN [1] {ECO:0000313|RefSeq:XP_006019028.1, ECO:0000313|RefSeq:XP_025054095.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (APR-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_006019028.1; XM_006018966.2.
DR RefSeq; XP_025054095.1; XM_025198310.1.
DR STRING; 38654.A0A1U7RJ56; -.
DR GeneID; 102386160; -.
DR KEGG; asn:102386160; -.
DR CTD; 1306; -.
DR eggNOG; KOG3544; Eukaryota.
DR eggNOG; KOG3546; Eukaryota.
DR Proteomes; UP000189705; 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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 6.
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_006019028.1};
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:UP000189705};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1303
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044566405"
FT DOMAIN 42..230
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 225..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..407
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..496
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..683
FT /note="Basic and acidic 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 816..832
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..857
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..986
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1019
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1303 AA; 134474 MW; 81BC83D58E05B051 CRC64;
MFKKMHSWNY WWSWNLLLVL LSSSLPVVLS AQVIEERGSK GHLDLTELIG VPLPPSVYFI
TGYGGFPAYS FGPDANIGRL TRALIPQPFY RDFAIVVTVK PNSNHGGVLF AITDAFQKTI
YLGMRLSPVD DGTQRIIMYY TEPGSHISRE AASFKVPVMT NKWNRFTVTV QGNDMALFMD
CEEYQRVQFQ RSAQALEFDS SSGIFVGNAG ATGLEKFTGS VQQLTIKPDP RATEDQCEDD
DPYASGDTSG NGSIQEQEGV PETQEAIASS QPPSDDTTAE PVEPPPTVSP HSEEMDFSGH
HILEETSVAP TIKKQGSDDE GNDQHENEAT IDTQEILKPE VGSGAHILQE ASREKGQKGE
KGQKGVQGPA GSPGKSRLKE MQTGIQGPPG LPGKPGQDGQ PGIPGKDGLP GKRGLQGVPG
MKGEMGMKGQ KGDPGVGIPG PPGLPGPPGP SAVPRRLSRL DPEGSGSGDL DRDHELFRGL
PGPPGPPGLP GLPGKPGPDS NTGPPGSPGE DGKNGASGEP GLPGPTGHPG LHGMVGPPGV
KGEKGDPGLS VSIGPKGDAG DTGAPGLKGE AGADGQPGKP GPPGLPGPPG PGYGFGFEDM
EGSGNIGLLS EPRTPGSRRP HGPVGEIGQR GPMGPKGEKG DAGPPGLTGL KGIQGASGKP
GFPGVSGRPG DEGPKGEKGD TGPKGEPGQD GASIVGPPGL PGPPGPIIAI PELPLNNTDG
IFNFTGIERL LGPPGPDGKP GLPGFPGPQG PKGDAGLRGL QGPKGQQGEK GEPGVNIAAD
GSLTKLMRRK GQKGEPGVLG PAGPMGPIGP SGPKGELGFP GRPGRPGLNG LKGVKGEKGE
TYGPPGLPGP PGPPGPPGHI AYIKGTVFPV SPRPHCKMPV STVYPGDQGS LDIHGFKGER
NSWGLNGPTG LKGEKGDQGS PGPPGPSLPS SYFSHFINSI KGEKGDSGEP GLKGEKGEPN
GGFFMTGPPG PPGRPGLVGP KGDSVVGPGG PPGLPGLPGS PGYGKVGPPG PPGPPGPPGP
PAIYGSAAAI PGPPGPPGEP GLPGTRNLVT TFRNIEGMLQ KAHLVAEGTL IYLRENSEVF
IRVRDGWRKL QLGELIPIPA ESPPPPAVSS HGFQSLPALT TFSNINTGKP SLHLVALNFP
FSGDMRADYQ CFQQARAAGL TSTYRAFLSS HLQDLSTVVR KADRYSLPIV NLKGEILFAN
WESIFTGNGG EFSIQIPIYS FDGKNVMTDP AWPQKIMWHG STANGIRLVS NYCEAWRTAE
IVAVGQASPL KAGKLLDQKA YSCSNRFIVL CIENSFISDI QRK
//
