ID A0A3Q7NLG2_CALUR Unreviewed; 1722 AA.
AC A0A3Q7NLG2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_025719177.1};
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_025719177.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025719177.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025719177.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: May regulate extracellular matrix-dependent motility and
CC morphogenesis of endothelial and non-endothelial cells; the function
CC requires homotrimerization and implicates MAPK signaling.
CC {ECO:0000256|ARBA:ARBA00053766}.
CC -!- FUNCTION: Probably plays a major role in determining the retinal
CC structure as well as in the closure of the neural tube.
CC {ECO:0000256|ARBA:ARBA00054383}.
CC -!- SUBUNIT: Forms homotrimers. Recombinant non-collagenous domain 1 has
CC stronger affinity to NID1, HSPG2 and laminin-1:NID1 complex and lower
CC affinity to FBLN1 and FBLN2 than endostatin.
CC {ECO:0000256|ARBA:ARBA00065165}.
CC -!- SUBUNIT: Monomeric. Interacts with KDR/VEGFR2. Interacts with the
CC ITGA5:ITGB1 complex. Interacts with NID1, HSPG2, laminin-1:NID1
CC complex, FBLN1 and FBLN2. {ECO:0000256|ARBA:ARBA00064471}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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_025719177.1; XM_025863392.1.
DR CTD; 80781; -.
DR Proteomes; UP000286641; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 1.10.2000.10:FF:000017; Alpha 1 type XVIII collagen; 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; 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: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; 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 3: Inferred from homology;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_025719177.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1722
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018531589"
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..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1540
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 1295..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1516
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 1722 AA; 174722 MW; 7D7E751180F6C5F3 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 PIYDSNAFME SGRPGPPGLP
GLQGPSGLKG DKGDVGPPGP PGQFPFDLLQ LGTEMKGEKG DRGDTGQKGE QGAPGGGGFF
GSSVPGPPGP PGYPGIPGPK GESIRGQPGP PGPQGPPGIG HEGRQGPPGP PGPPGPPGPP
SFPGPYRQTI SVPGPPGPPG PPGPPGTMGT SSGQVRIWAT YQTMLDKVPE VPEGWLIFVA
EREELYVRVR NGLRKVLLGP RTPLPRGTDN EVAALQPPVG NPYPRRELTH STARPWRADD
ILASPPRLPD PQPYPGAPQH GSYLHFQPAR PTGGPTHTHT HQDYHPVLHL VALNSPQPGG
MRGIRGADFQ CFQQARAVGL AGTFRAFLSS RLQDLYSVVR RADRTSVPIV NLRDEVLFPS
WEALFSGSEG RLKPGARIFS FDGRDVLQHP AWPQKSVWHG SDPSGRRLTD SYCETWRTEA
AAATGQASSL LAGRLLAQKA TGCHNTLIVL CIENSFMTSF SK
//
