ID A0A1U8C1A8_MESAU Unreviewed; 1518 AA.
AC A0A1U8C1A8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 28-JAN-2026, entry version 42.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X2 {ECO:0000313|RefSeq:XP_012969354.1};
GN Name=Col18a1 {ECO:0000313|RefSeq:XP_012969354.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000886700, ECO:0000313|RefSeq:XP_012969354.1};
RN [1] {ECO:0000313|RefSeq:XP_012969354.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_012969354.1};
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_012969354.1; XM_013113900.2.
DR GeneID; 101836799; -.
DR KEGG; maua:101836799; -.
DR CTD; 80781; -.
DR eggNOG; KOG3546; Eukaryota.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000886700; 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; 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; PF13385; Laminin_G_3; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_012969354.1};
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:UP000886700};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1518
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010534108"
FT DOMAIN 235..423
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 49..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..118
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..533
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..707
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..726
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..785
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..824
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..859
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..891
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1033
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1061
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1518 AA; 155310 MW; 874B658DFE3813C8 CRC64;
MAPDPSRRLW LLLLLLLSCC LEPARPDRNP LNPLNPLSPL VWLWSTKTND PISEPKSSSP
VEPTESPTTH AVPQDGLAEQ QTARANPKLP PEDQEAGQSG TPTTTATPIP PMASAASPDM
KEENVAGVGA KILNVAQGIR SFVQLWDENP ATKKSAGMEA SASSIPSALL TPTEFSSAPQ
EGDTTLWLNR GVPSSPDVQT TEAGTLTVPT QPPPSLSSLQ APLRRPTPPE NVAEEVGLPQ
LLGDPLPQQI TQIDDPHVGP VYIFGRDSSS SQTAQHHFPR LFFRDFSLLF HIQPATKAAG
VLFAITDTVQ KVVSLGVKLS GVQNGHQNIS LLYTEPGATQ TQTGASFHLP AFVGQWTHFV
LSVDGGSVTL YVDCEEFQRV PFARSPQGLE LEHGSGLFVG QAGAADPDKF QGKISELKVR
QNPRVSPVLC SDEDGDDEDR ASGDFGSGFE ESSKPHREED TSLAPSLPQP PPVTSPPLAG
GSTTEDSRTE ETEEETTVDS IGAETLPGTD SSRARDESVQ NHGGGLIKGG LKGQKGEPGA
RGLPGPAGPQ GPAGPVIQSP IAQPVPGAQG PPGPQGPPGK DGAPGRDGEP GDPGEDGRPG
DAGPQGFPGT PGDVGPKGEK GDPGVGARGP PGPPGPPGPS FRQDKLTFID MEGSGFSGDL
ESLRGPRGFP GPPGPPGVPG LPGEPGRFGV NSSYAPGPAG LPGVPGKEGP PGFPGPPGPP
GPPGKVGPPG EAGQKGNVGE VGIPGPKGSK GDLGPVGVPG KTGMAGPPGP TGPPGPPGPP
GPPGPGFAAG FDDMEGSGIP FWSTARSSEG LQGPPGLPGL KGDPGVTGPP GAKGEVGAEG
VQGMPGLPGR AGAAGSPGPK GEKGSQGEKG SPGKDGVGLP GLPGPPGPPG PVLYVSNEDR
AVVTTPGPEG KPGYAGFPGP AGPKGDLGSK GEQGLPGPKG EKGEPGAIFG PDGRALGHAQ
KGAKGEPGFR GPPGPYGRPG HKGEIGFPGR PGRPGTNGLK GEKGEPGDAS LGFSMRGLPG
PPGPPGPPGP PGMPIYDSNA FVESGRPGLP GQQGVQGPSG PKGDKGEVGP PGPPGQFPID
FFNLGAEMKG DKGDRGDTGQ KGERGEPGVA GGGFFSSSVP GPPGPPGYPG IPGPKGESIR
GPPGPPGPQG PPGIGYEGRQ GPPGPPGPPG PPSFPGPHRQ TVSVPGPPGP PGPPGPPGAM
GASAGQVRIW ATYQTMLDKV REVPEGWLIF VAEREELYVR VRNGFRKVLL EARTALPHGT
GNEVAALQPP LVQLHEGSPY TRREHSYSTA RPWRADDILA NPPRLPEPQP YPGVPHHHSS
SVHQPPAHPT GSPAHTHHDF QPVLHLVALN SPLSGGMRGI RGADFQCFQQ ARAVGLAGTF
RAFLSSRLQD LYSIVRRADR GTVPIVNLKD EVLSPSWDAL FSGSQGQLQP GARIFSFDGR
DVLRHPVWPQ KSIWHGSDPS GRRLMESYCE TWRTEATGAT GQASSLLSGR LLEQKAASCH
NTYIVLCIEN SFMTSFSK
//
