ID A0A2Y9QBG9_DELLE Unreviewed; 1785 AA.
AC A0A2Y9QBG9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_022452792.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022452792.1};
RN [1] {ECO:0000313|RefSeq:XP_022452792.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022452792.1};
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_022452792.1; XM_022597084.2.
DR FunCoup; A0A2Y9QBG9; 89.
DR STRING; 9749.A0A2Y9QBG9; -.
DR GeneID; 111186452; -.
DR KEGG; dle:111186452; -.
DR CTD; 80781; -.
DR InParanoid; A0A2Y9QBG9; -.
DR Proteomes; UP000248483; 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:0032836; P:glomerular basement membrane development; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF714; COLLAGEN ALPHA-4(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
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_022452792.1};
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:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 372..489
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 79..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..142
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..829
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..907
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..974
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1022
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1097
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1193
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1397
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1588
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 387..433
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 424..462
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1785 AA; 181429 MW; 6841802D4D36BA39 CRC64;
MNGELAAGPG AGGGGGLAPP LDGRGRRLLC GAHSLMAPDP SGRRGHCGLL LLLACCLAPT
RADLMSWLWS ADTAGSTVTL ASKPPGSSPV RPTEDTSTHV APQDDPTQQW KALASPEPPL
ERPEVGQGQA PTVPSAPSTA SPDTKEENIA GVGAKILNVA LGIRSFVQLW DDTTPTKSSA
RAGTPGPENL TDPLTTPGPS SGPQDDWTTL WLSTGAPSSP DTQRTEAGTL PAPTQPPPSP
DRPRALLGEP AVPPPSPGRA SLSSARAGAP PQGSQPPPGW PQELDSKGLL PAAARPGQQH
RRPDDRTHTP PPLALVTGSP GVHAGRWALS SDPSAKLSHA ALLALSGDRG AWVPHVANPA
GPGLADSSAL LGAAGRCLPL LPSLALCGHL GIGRFWLPNH LHHASGEEVQ AAVRAWGALL
QTHCHRFLAW FFCLLLAPPC GPGALPGPPP CRQFCEALED ACWSRLDGRG LPFPCASLPA
REDGRCVFIG PPAESQVMEV GLQPLLGEPL PQQVALVHDP DVGPAYEFGA DVGGDGWVAR
SLLPSTFFQH FSLLVHVRPA SARAGVLFAV TDAAQAVVLV GLKLAAARGA WQQVQLLYTE
PGAARTHTAA SFTLPTLDGR WTRLAIAVDG AHATLFVDCK EVQRQPLTRS PRGLQLEPDA
RLFVAQAGRA DPDKFQGLVS DLRLREDPQV SPLHCLGEDE KDDDDRASGD LGSGLAETWE
RIGEELGAPL GPGLPEAPPV TSPPLAGVGS QEDFRTEEIE EETTVSSLGA QTLPSLSTVA
TWDGGEWSPG GGLKEQGLKG QKGEPGAQGP PGPVGPQGPS GPAVQSPDAQ PVPGPQGPPG
PPGKDGAPGR DGEPGDPGED GKPGDTGPQG FPGTPGDMGP KGEKGDPGVG PRGPPGPQGP
PGPPGPSFRP DRLTFIDMEG SGFGGDLESL RGPRGFPGPP GPPGVPGLPG EPGRFGMNSS
DVPGPAGLPG VPGRDGPPGL PGTPGPPGPP GKDGQPGQTG QKGSLGEAGA PGPKGSKGDP
GPIGMPGEHG LAGRPGPAGP PGPPGPPGPP GPGLAAGFDD MEGSGGPFWS TARGANGPQG
PPGPPGVQGD PGVMGPPGTK GEAGADGAPG FPGLPGRDGA AGLQGPKGEK GPQGEKGDPG
KDGVGQPGLP GPPGPPGPVV YVSEQDRALA SVPGPEGWVG LAGLPGPAGP KGDLGSRGQQ
GLLGPKGEKG EPGMVFSPDG RALTSAQKGA KGEPGFRGPP GPYGRPGHKG EIGFPGRPGR
PGMNGLKGEK GEPGDASVGF SARGPPGPPG PPGPPGPPGT PVYDSNAFVE SGRPGPPGLP
GHQGPSGPKG DKGEVGPPGP PGQFPLDLLH LGAEMKGEKG DQGAAGQKGE RGEPGGGGFF
GSSVPGPPGP PGYPGIPGPK GESIQGQPGP PGPQGPPGIG YEGRQGPPGP PGPPGPPGPP
SFPGPYRQTI SVPGPPGPPG PPGPPGSMGT SSGQVRVWAT YQTLLDQVPA VPEGWLIYVA
DREELYVRVR NGFRKVLLEA RTPLPRGTDN EVAALQPPVV QLHEGNPYPR REPPHPTARS
WRADDILASA PRLTHAQPYP GAPHPGAYAH HRPATPTASP AHTHHDFQPV LHLVALNSPQ
SGGLRGIRGA DFQCFQQARA AGLAGTFRAF LSSRLQDLYS IVRRADRATL PIVNLRDEVL
SPSWEALFSG SEGQLKPGAR IFSFDGRDVL QHPAWPQKSL WHGSDPSGRR LTESYCETWR
TEARAATGQA SSLLAGRLLE QKAASCYNAF IVLCIENSFM TSSSK
//
