ID A0A8B8X8Q2_BALMU Unreviewed; 1752 AA.
AC A0A8B8X8Q2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_036705929.1};
OS Balaenoptera musculus (Blue whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=9771 {ECO:0000313|Proteomes:UP000694857, ECO:0000313|RefSeq:XP_036705929.1};
RN [1] {ECO:0000313|RefSeq:XP_036705929.1}
RP IDENTIFICATION.
RC TISSUE=Epidermis and Blubber {ECO:0000313|RefSeq:XP_036705929.1};
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_036705929.1; XM_036850034.1.
DR GeneID; 118894177; -.
DR CTD; 80781; -.
DR Proteomes; UP000694857; Chromosome 4.
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_036705929.1};
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:UP000694857};
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..1752
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034055664"
FT DOMAIN 337..454
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 40..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..107
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..237
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..794
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..911
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..939
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..955
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1000
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1020
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1094
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1173
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1266
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1433
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 352..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 389..427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1752 AA; 177892 MW; 9D6D9EA04C3230D4 CRC64;
MAPDPSGRRG HCGLLLLLAC CLAPARADLM SWLWPGNAAG STVAPASTPP GSSPVRPTED
TTTHVAPQDD PTQQWKALAS PEPPLERPEV GQGQAPAVPS AVSTASPDTK EENIAGVGAK
ILNVALGIRS FVQLWDDTTP TESSATAGTP GPGNPTDPLT TPGPSSGPQD GGTTVWLSTG
APSSPDAQRT EAGTLPAPTQ PPPSPDRPRA LLREPAVPPP SPGRPSLSSA RAGAPPQGSQ
PPPGWPQELD SEGLSPAAAR PGQRHRRPDD RTRTPPPLAL VTGSPGAHAG PWALSSDPSA
KLSHAALVAL SGDRGAWVPR VANPAGPGLA DSSALLGAAG RCLPLLPSLA LCGHLGVGRF
WLPNHLHHAS GEEVQAAARA WGALLQTHCH RFLAWFFCLL LAPACGPGAL PGPPPCRQFC
EALEDACWSR LDGRGLPFPC ASLPAREDGR CVFIGPPADS QVMEVGLQLL LGEPLPRQVA
LVHDPDVGPA YEFGVDVGGD GWAARSLLPS TFFRRFSLLV RVRPASARAG VLFAVTDAAQ
AVVLVGVKLA AARGAWQQVQ LLYTEPGAAR THTAASFALP ALDGRWTRLA LTVDGTHAAL
FVDCKEVQRQ PLARSPRGLQ LEPDARLFVA QAGRADPDKF QGLISDLRLR EEPQVSPLHC
LDEDEEDDDD RASGDLGSGL AETWEHIGEE LGAPLGPRLP EAPPVTSPPL AGVGNQEDFR
TEETEEETTV SSLGAQTLPS LSTVTTWAGS EWSPGRGLKE GGLKGQKGEP GAQGPPGPVG
PQGPAGPAVQ SPDAQPVPGP QGPPGPPGKD GAPGRDGEPG DPGEDGKPGD TGPQGFPGTP
GDVGPKGEKG DPGVGPRGPP GPQGPPGPPG PSFRHDRLTF IDMEGSGFGG DLESLRGPRG
VPGPPGPPGV PGLPGEPGRF GMNSSDVPGP AGLPGVPGRD GPPGLPGPPG PPGPPGKDGR
PGQTGQKGSL GEAGAPGPKG SKGDPGPIGT PGEHGLAGHP GPAGPAGPPG PPGPPGPPGP
GLAAGFDDME GSGGPFWSTA RGASGPQGPL GPPGVKGDPG VMGPPGTKGE VGADGAPGAP
GLPGREGAAG LQGPKGEKGP QGEKGDPGKD GVGQPGLPGP PGPPGPVVYV SEQDRALASV
PGPEGRAGLA GLPGPAGPKG DLGSRGQQGL PGPKGEKGEP GMVFSPDGRA LTSAQKGAKG
EPGFRGPPGP YGRPGHKGEI GFPGRPGRPG MNGLKGEKGE PGDASVGFSA RGPPGPPGPP
GPPGLPGTPV YDSNAFVESG RPGPPGLPGN QGPSGPKGDK GEVGPPGPPG QFPFDLLHLG
AEMKGEKGDQ GAAGQKGERG EPGGGGFFSS SMPGPPGPPG YPGIPGPKGE SIQGQPGPPG
PQGPPGIGYE GHQGPPGPPG PPGPPGPPSF PGPYRQTISV PGPPGPPGPP GPPGSMGTSS
GVRVWATYQT LLDQVPEVPE GWLVYVADRE ELYVRVRNGF RKVLLEARTP LPRGTDNEVA
ALQPPVVQLH EGNPYPRREP PPPTARSWRA DDILAGPPRL THAQPYPRAP HPGAYAHLRP
ATPTASPAHT HHDFQPVLHL VALNSPQSGG LRGIRGADFQ CFQQARAAGL AGTFRAFLSS
RLQDLYSIVR RADRAALPIV NLRDEVLSPS WEALFSGSEG QLKPGARIFS FDGRDVLQHP
AWPQKSLWHG SDPSGRRLTE SYCETWRTEA RAATGQASSL LAGRLLEQKA AGCYNAFIVL
CIENSFMTSS SK
//
