ID A0A4W3JG75_CALMI Unreviewed; 1315 AA.
AC A0A4W3JG75;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE SubName: Full=Collagen alpha-1(XV) chain-like {ECO:0000313|Ensembl:ENSCMIP00000037028.1};
GN Name=LOC103181551 {ECO:0000313|Ensembl:ENSCMIP00000037028.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|Ensembl:ENSCMIP00000037028.1, ECO:0000313|Proteomes:UP000314986};
RN [1] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17185593; DOI=10.1126/science.1130708;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Ancient noncoding elements conserved in the human genome.";
RL Science 314:1892-1892(2006).
RN [2] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17407382;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Survey sequencing and comparative analysis of the elephant shark
RT (Callorhinchus milii) genome.";
RL PLoS Biol. 5:E101-E101(2007).
RN [3] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
RN [4] {ECO:0000313|Ensembl:ENSCMIP00000037028.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [5] {ECO:0000313|Ensembl:ENSCMIP00000037028.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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; ENSCMIT00000037569.1; ENSCMIP00000037028.1; ENSCMIG00000015600.1.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000314986; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 4.
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; 1.
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:UP000314986};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1315
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021413025"
FT DOMAIN 30..218
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 79..217
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 215..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..494
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..557
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..679
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..889
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1043
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1315 AA; 133248 MW; 8BAA0A9F6A1071FB CRC64;
MLLLLLLWTW SCCRLTSSAR LMEERGSIGH LDLTGLIGVP LPANVSFITG YEGFPAYSFG
LGVNIGRLTR TMIPSRFYRD FAILVTIRPE SENGGVLFAI TNAFQSIIYL GLKLTSVWNG
SQRIVLFYTE RSYQASHEVA SFEVPAMTNK WTRFALSIQD NLVTLYLDCE EDQRSYMKRS
SQPLVFDSSS GIFIGNAGAS GLNNFVGSIQ QLTIKSDPRA SEEQCEEEEP YGSGEGSGEG
SGYDSHQVQA GTRAQIQTAT PQTIREDTLI GEPFKAPPTV EPLAVEIEGP SGQLESMLQE
VLPSGTSGES PYSGHLEFGV EGEKGAPGQK GETGDLGPPG PKGEIESGSG NLQTEIGEKG
EKGDPGSKGK SGVGSPGLKG EKGEAGLPGI PGSPGPVVVP TVPAIPGPPG PLGPPGLPGK
DGPKGVPGKD GKHGEQGPAG FPGTPGDLGP KGEKGDPGFS GHPGLPGLPG PPGPPGPSTQ
LGVLGVSEGS GVDGFVDSDM EVTRGSPGLP GLPGPPGLPG IPGLPGHPDK AKVMDSYLVG
SSASPGAPGQ PGQDGASGEP GPRGPSGLDG VAGPAGPKGD KGDHGLPGLQ GAKGDMGDNG
LPGPAGKPGQ PGKEGPMGPP GPPGPPGPSR ASGREGSGIS SGFEDMEGSG AFGLPGIPGK
AGLPGPQGPP GAKGDAGPSG EKGASGFPGQ EGEIGQAGLP GPMGPRGEKG EAGLKGERGL
DGVGNPGLPG QPGPPGPIVS LQDLLLNDTK ALFNFSVQAL PGPPGPEGMP GHAGFPGPRG
PKGDLGLTGP PGVKGEKGEP GASIAADGSL MALTGVQGPK GQKGSPGFMG PQGPMGPRGF
PGSKGEFGLP GRLGRPGKHG VPGQKGEAVI SQGNPGLPGP PGLPGPPGPV LNLKGVNGEP
GQQTAINFLG PKGQKGSVGF PGNGGSKGDK GDQGSPGPPG PYSFLGSYGN GHKGEKGDGG
AMGPKGDKGD SGGLFMPGSR GPTGPPGRPG PVGPKGESIE GPMGPPGRSG VPGSPGYGIV
GPPGRPGPPG SPGAAGVFGS AVALPGPPGP PGPPGPPSTG SPVTIFKNVD LMHKTTYIVS
EGSLGYVSER GDLYIRVYNG WRKLQLGDLV PAPADDPFNA LNYLPAPNSF PKINNEKPAL
HLVALNTPLS GNMQGIRGAD FHCFQQARAM GSMATYRAFL SSHLQDLYTI VRKADRVKMP
IVNLKGEVLF ANWEAIFKSR AAFDTNIPIY SFDGRNIMKD PSWPHKIIWH GSNENGAGVP
TNYCQAWRRA DMVITGKASP LSSGKLLVQH LYNCANNFVV LCIENSYMHD QRRRK
//
