ID A0A3Q7PT92_CALUR Unreviewed; 1780 AA.
AC A0A3Q7PT92;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X3 {ECO:0000313|RefSeq:XP_025719176.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_025719176.1};
OS Callorhinus ursinus (Northern fur seal).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Otariidae;
OC Callorhinus.
OX NCBI_TaxID=34884 {ECO:0000313|Proteomes:UP000286641, ECO:0000313|RefSeq:XP_025719176.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025719176.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025719176.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR RefSeq; XP_025719176.1; XM_025863391.1.
DR CTD; 80781; -.
DR Proteomes; UP000286641; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR FunFam; 1.10.2000.10:FF:000017; Alpha 1 type XVIII collagen; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 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; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR010363; DUF959_COL18_N.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
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; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 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.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_025719176.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000286641};
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..1780
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018661734"
FT DOMAIN 338..455
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 43..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1728..1780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..228
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..255
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..279
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..706
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..846
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..886
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..920
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..930
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..940
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..975
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1037
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1098
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1376
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1487
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1746
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 353..399
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 390..428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1780 AA; 181404 MW; AC3DB7516B6213A3 CRC64;
MARLPGSRLG PPLLLLLVTC CLTAARADLL SLNWLWSTRT DGPTAELVSE PPGSPHGQPR
EDTGTRAAPQ HGPTEQGRAP ASSELPAERP EPGPGGTSPA GPDTKEENIA GVGAKILNVA
QGIRSFVQLW DDATPTTSPP GAEAPAPVTP TPPLTLPGPS SAPQENGTAL WLGSGAPSSP
DTQRTEAGTL PVPTQLPPFL GGRSPPPPAA GRASPSSAPG GAPPWGSRQS PGWPQDPDSG
GLLRMAARPG QQRRPPGIRR RTPPLLPLVT GPLGALTGPS ARSSDPPTLV SQIPLSAGPG
AGGARAPHVA NSVGPGLANR SALLGADPLT PAGQPVPAAG GRCLPLPPSL PACSHLGIGR
AWLPNHLRHG SSEEVRAAAR AWGHLLQTHC HRFLAWFFCL LLAPPCGAGP PPAPPPCRQF
CEALEDACWG HLDGGGLPVS CASLPAQEDG LCVFIGPGAE SLGTEVGLLQ LLGEPPPPQV
TQVEDPDVGP AFVFGLDANS GQVARYHFPS PFFRDFSLHF HVRPATEDAG VLFAITDAAQ
AVVSVGVRLS GVRDGHQHIQ LLYTEPGATR THTAASFRLP AFTGQWTRFA LSVDGATVAL
FVDCELFQRV PLVRSPRGLE LEPGAGLFVA QAGGADPDKF QGVIAELRVR GDPHVSPLHC
LEEDDEGGGR VSGDFGSGLE ETREPLREQS GPSPKPSLPE APPVTSPPLA AGRDVEDSRT
EEIEEETTVS SLGARIRPGL EAVTTGSVWS PGGGLEEGPA VQSPHAWPVP GPQGPPGPLG
PPGKDGAPGR DGEPGDPGED GRPGDPGPQG FPGTPGDAGP KGEKGDPGVG PRGPPGPQGP
PGPPGPSFRH DKLTFIDMEG SGFGGDLESL RGPRGFPGPP GPPGVPGLPG EPGRFGMNSS
DVPGPAGLPG VPGRDGAPGL PGTPGPPGPP GKEGGPGKMG QKGSPGEVGA PGPKGSKGDP
GPVGAPGENG LAGAPGPAGP PGPPGPPGPP GPELAAGFDD MEGSGGPFWS TAQGASGSQG
PPGPPGIKGD PGITGPPGAK GEVGAEGPPG FPGLPGREGS AGAQGPKGEK GTQGEKGDPG
RDGVGQPGLP GPPGPPGPVV YMSEQDKVLG GVPGPEGRPG FAGFPGPAGP KGDLGSKGQR
GLPGPKGEKG EPGPLFSPDG SMLAPAQKGA KGEPGFRGPP GPYGRPGHKG EIGFPGRPGR
PGMNGLKGEK GEPGHSSIGF GMRGPPGPPG PPGPPGPPGT PIYDSNGSRG LLDSRVTKEM
WALQDHQGEK GDRGDTGQKG EQGAPGGGGF FGSSVPGPPG PPGYPGIPGP KGESIRGQPG
PPGPQGPPGI GHEGRQGPPG PPGPPGPPGP PSFPGPYRQT ISVPGPPGPP GPPGPPGTMG
TSSGQVRIWA TYQTMLDKVP EVPEGWLIFV AEREELYVRV RNGLRKVLLG PRTPLPRGTD
NEVAALQPPV GNPYPRRELT HSTARPWRAD DILASPPRLP DPQPYPGAPQ HGSYLHFQPA
RPTGGPTHTH THQDYHPVLH LVALNSPQPG GMRGIRGADF QCFQQARAVG LAGTFRAFLS
SRLQDLYSVV RRADRTSVPI VNLRAPEERV ARLRPQRTPA DRQLLRDVAD RGCSSHGPGV
LAAGWPAAGA ESHGLPQHPH CALHREQLHD LLLQVGALPA QTDRRTWGQR GGPGEWRSCC
AGASAHPPRV GTQLGHFPVW FTAYGSPSRN KRKPKSVFLK KFKTKPGART LLRPSPPHTG
PCPLPSWPQS DQGVDPGHGK GTHYPRGWGA PAAFRGPHRC
//
