ID A0A7F8R4I0_LEPWE Unreviewed; 1473 AA.
AC A0A7F8R4I0;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X4 {ECO:0000313|RefSeq:XP_030888096.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_030888096.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Monachinae; Lobodontini; Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_030888096.1};
RN [1] {ECO:0000313|RefSeq:XP_030888096.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_030888096.1};
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_030888096.1; XM_031032236.1.
DR GeneID; 102733383; -.
DR CTD; 80781; -.
DR Proteomes; UP000245341; 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: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; 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; IPR010363; DUF959_COL18_N.
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 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_030888096.1};
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:UP000245341};
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..1473
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028906582"
FT DOMAIN 216..404
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 265..403
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 44..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..158
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..457
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..665
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..681
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..691
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..726
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..849
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..991
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1088
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1473 AA; 149635 MW; A7B606457BD1FF91 CRC64;
MARLPGGRLG PPLLLLLVTY CLAAAHADLL SLNWLWSTRT DGPTAELVSE PPGSPHGQPR
EDTSTHAAPQ HGPTEQGRGP ASSELPVERP ETGLGGASPA GPDTKEENIA GVGAKILNVA
QGIRSFVQLW DDATPTTSPP GTEAPAPVTP TAPLTLPGPS SPPQENGTAL WLGSGAPSSP
DTQRTEAGTP PVPTQLPPFP GGPSPPPPAA ESLGTEVGLL QLLGEPPPPQ VTQVDDPDIG
PAFVFGPDAN SGQVARYHFP SPFFRDFSLH FHVQPATEDA GVLFAITDAA QAVVSVGVRL
SGVRDGHQHI QLLYTEPGAT RTHTAASFRL PAFTGQWTRF ALSVDGATVA LFVDCELFQR
VPLVRSLRGL ELEPGAGLFV AQAGGADPDK FQGMIAELRV RGDPHVSPLH CLEEDDEDSG
GVSGDFGSGL EETREPLREQ SGPSPKPSLP EAPPVTSPPL AAGRDVEDSR TEEIEEETTV
SSLGARTLPG LDAVTIESVR SAGGGLEEGP AVHSPDARPI PGPQGPPGPP GPPGKDGAPG
RDGEPGDPGE DGRPGDPGPQ GFPGTPGDAG PKGEKGDPGV GPRGPPGPQG PPGPPGPSFR
HDKLTFIDME GSGFGGDLES LRGPRGFPGP PGPPGVPGLP GEPGRFGMNS SDVPGPAGLP
GVPGRDGPPG LPGTPGPPGP PGKDGGPGKM GQKGSPGEVG APGPKGRQGD PGPVGAPGEN
GLAGAPGPAG PPGPPGPPGP PGPGLAAGFD DMEGSGRPFW STAQGASGSQ GPPGPPGVKG
DPGITGPPGA KGEVGADGPP GFPGLPGREG SAGAQGPKGE KGTQGEKGDP GRDGVGQPGL
PGPPGPPGPV VYMSEQDRVL GGVPGPEGRP GFAGFPGPAG PKGDLGSKGQ RGLPGPKGEK
GEPGPVFSPD GSLLAPAQKG AKGEPGFRGP PGPYGRPGHK GEIGFPGRPG RPGMNGLKGE
KGEPGHSSIG FGMRGPPGPP GPPGPPGPPG TPIYDSNAFM ESGRPGPPGL PGLQGPSGPK
GDKGDVGPPG PPGQFPFDLL QLGTEMKGEK GDRGDTGQKG ERGEPGGGGF FGSSVPGPPG
PPGYPGIPGP KGESIRGQPG PPGPQGPPGI GHEGRQGPPG PPGPPGPPGP PSFPGPYRQT
ISVPGPPGPP GPPGPPGTMG TSSGQVRIWA TYQTMLDKVP EVPEGWLIFV AEREELYVRV
RNGLRKVLLE ARMPLPHGTD NEVAALQPPV GNPYPRRELT HSTARPWRAD DILASPPRLL
DPQPYPGAPQ HGSYLHFQPA RPTGRPTHTH THQDYHPVLH LVALNSPQPG GMRGIRGADF
QCFQQARTVG LAGTFRAFLS SRLQDLYSIV RRADRTSVPI VNLRDEVLFP SWEALFSGSE
GQLKPGARIF SFDGRDVLQH PAWPQKSVWH GSDPSGRRLT DSYCETWRTE AGAATGQASS
LLAGRLLAQK AASCHNAFIV LCIENSFMTS FSK
//
