ID A0A3Q7NLG7_CALUR Unreviewed; 1297 AA.
AC A0A3Q7NLG7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X9 {ECO:0000313|RefSeq:XP_025719182.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_025719182.1};
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_025719182.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025719182.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025719182.1};
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_025719182.1; XM_025863397.1.
DR GeneID; 112816720; -.
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 GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 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; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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 ECO:0000313|RefSeq:XP_025719182.1};
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: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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1297
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018547570"
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 90..228
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 231..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..496
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..516
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..551
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..613
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..674
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..913
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..959
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..981
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1091
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1297 AA; 131933 MW; 774DA635570336DB CRC64;
MAPRWPWLRP RPRSLLDVLA PVVLLLGVRV ASAEPESLGT EVGLLQLLGE PPPPQVTQVE
DPDVGPAFVF GLDANSGQVA RYHFPSPFFR DFSLHFHVRP ATEDAGVLFA ITDAAQAVVS
VGVRLSGVRD GHQHIQLLYT EPGATRTHTA ASFRLPAFTG QWTRFALSVD GATVALFVDC
ELFQRVPLVR SPRGLELEPG AGLFVAQAGG ADPDKFQGVI AELRVRGDPH VSPLHCLEED
DEGGGRVSGD FGSGLEETRE PLREQSGPSP KPSLPEAPPV TSPPLAAGRD VEDSRTEEIE
EETTVSSLGA RIRPGLEAVT TGSVWSPGGG LEEGPAVQSP HAWPVPGPQG PPGPLGPPGK
DGAPGRDGEP GDPGEDGRPG DPGPQGFPGT PGDAGPKGEK GDPGVGPRGP PGPQGPPGPP
GPSFRHDKLT FIDMEGSGFG GDLESLRGPR GFPGPPGPPG VPGLPGEPGR FGMNSSDVPG
PAGLPGVPGR DGAPGLPGTP GPPGPPGKEG GPGKMGQKGS PGEVGAPGPK GSKGDPGPVG
APGENGLAGA PGPAGPPGPP GPPGPPGPEL AAGFDDMEGS GGPFWSTAQG ASGSQGPPGP
PGIKGDPGIT GPPGAKGEVG AEGPPGFPGL PGREGSAGAQ GPKGEKGTQG EKGDPGRDGV
GQPGLPGPPG PPGPVVYMSE QDKVLGGVPG PEGRPGFAGF PGPAGPKGDL GSKGQRGLPG
PKGEKGEPGP LFSPDGSMLA PAQKGAKGEP GFRGPPGPYG RPGHKGEIGF PGRPGRPGMN
GLKGEKGEPG HSSIGFGMRG PPGPPGPPGP PGPPGTPIYD SNAFMESGRP GPPGLPGLQG
PSGLKGDKGD VGPPGPPGQF PFDLLQLGTE MKGEKGDRGD TGQKGEQGAP GGGGFFGSSV
PGPPGPPGYP GIPGPKGESI RGQPGPPGPQ GPPGIGHEGR QGPPGPPGPP GPPGPPSFPG
PYRQTISVPG PPGPPGPPGP PGTMGTSSGV RIWATYQTML DKVPEVPEGW LIFVAEREEL
YVRVRNGLRK VLLGPRTPLP RGTDNEVAAL QPPVGNPYPR RELTHSTARP WRADDILASP
PRLPDPQPYP GAPQHGSYLH FQPARPTGGP THTHTHQDYH PVLHLVALNS PQPGGMRGIR
GADFQCFQQA RAVGLAGTFR AFLSSRLQDL YSVVRRADRT SVPIVNLRDE VLFPSWEALF
SGSEGRLKPG ARIFSFDGRD VLQHPAWPQK SVWHGSDPSG RRLTDSYCET WRTEAAAATG
QASSLLAGRL LAQKATGCHN TLIVLCIENS FMTSFSK
//
