ID U3JMV0_FICAL Unreviewed; 2201 AA.
AC U3JMV0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 28-JAN-2026, entry version 71.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSFALP00000004104.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000004104.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000004104.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000004104.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSFALP00000004104.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 59894.ENSFALP00000004104; -.
DR Ensembl; ENSFALT00000004123.2; ENSFALP00000004104.2; ENSFALG00000003898.2.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000158212; -.
DR HOGENOM; CLU_004003_1_0_1; -.
DR Proteomes; UP000016665; Chromosome 7.
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; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1118; LAMININ G DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
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 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:UP000016665};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2201
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032900610"
FT DOMAIN 766..884
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 34..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..56
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1098
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1145
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1798
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1830
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1841..1854
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1864..1876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 781..827
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 818..856
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 2201 AA; 226395 MW; 80BB41F5DD0328D5 CRC64;
MAPPRLGFLL LLACCFSCSE PQLLDWVWDS AKTTGSPAAP GKGIPASEPP TSAAAPAPSP
SPVRWGGEAA GNVTTPRRQE PDPATAAPVG EGTTEQWDRS ATGLLESTAR ASIAPPHIMS
PAPGQQVASS PRNKPQLLGT GTPKDLQLLG SGTTEDPQLL GSGSTEDLQL LRMKTTKELQ
FLGSVSPTEH LGTGTTEDLQ LLGSGTTENP QLLGSGTSKD LQLLGSGTTE DLQLLGLGTT
EDLQLLGMVS TADLGSVSPK ELLGTGTTEN LQLLGSGTTE NPQLLGSGTS KDLQLLGSGT
TEDLQLLGLG TTEDLQLLGM VSTADLGSVS PKELLGTGTT ENLQLLGSGT TENPQLLGSG
TSKDLQLLGS GTTEDLQLLG LGTTEDLQLL GMVSTADLGS VSPKELLGTG TTENLQLLGS
GTTENPQLLG SGTSKDLQLL GSGTTEDLQL LGLGTTEDLQ LLGMVSTADL GSVSPKELLG
TGTTENLQLL GSGTTENPQL LGSGTSKDLQ LLGSGTTEDL QLLGLGTTED LQLLGMVSTA
DLGSVSPKEL LGTGTTENLQ LLGSGTTENP QLLGSGTSKD LQLLGSGTTE DLQLLGLGTT
EDLQLLGMVS TADLGSVSPK ELLGTGTTEN LQLLGSGTTE NPQLLGSGTS KDLQLLGSGT
TEDLQLLVME RTKDPQLLRT TKDPQLLGQG TTENLQLVAM RSTEETQLPR TVTSERPELL
GNTENPQLVR MVTTENPEFL GTGTPTAIET QVSLQRPAGP QTGLMPIAGR CQPIPTHLPV
CSVLGTSHVR LPNYLRHSSE EEIQAALHEW EGLLKSRCHR YLEWFLCLLL LPGCSPSVPV
TPPPCQGFCE AVRDLCWTHL AGGRLPLPCD ALPEEDEGVS CVFINASAES LSAEVSLLEL
IGDPLTEEIH RIYGPDNNPG YVFGPNANTG QVARYHLPSP FYRDFSLLFH IQPTTPRAGV
LFAVTDSSQS IIYVGVKLSE LRAGQQQIIF YYTEPGSPSS YPAATFTVPT LLNQWTRFAI
SVEEEEVILY LDCEEHERVR FERSPDEMEL EEGSGLFVAQ AGGADPDKYQ GVIADLKLRG
DPRAAERQCE EEEDDAEVSG DFGSGMEGGQ QPSGKVEAVP GLVDAVPVTS PPVAGGSGPR
SGGGSPQQAE RTRAEERLRV STGDTSRKGE KGEKGERGLK GDSGTSGIIG PGSVKGQKGE
KGDLGVKGSA GFGYPGSKGQ KGEPGDPGPP GTHSRHGDGL VVEQVTGPPG PPGKDGAPGR
DGEPGDPGED GKPGEMGPPG FPGMPGEPGL KGEKGDPGVG PRGPPGPPGP PGPPAPPSKN
DKLTFIDMEG SGFGGDLESL RGPRGPPGPP GPPGVPGLPG EPGRFGMNRT DLPGPPGLPG
RDGIPGPQGP VGPQGPPGRD GEAGQPGPKG EQGDVGDLGL PGLPGPKGSK GETGPAGPPG
EMGLAGLPGP IGPRGQPGPP GPPGPPGPGY EAGFSDMEGS GLPFTPGPPG PEGPQGVPGL
PGVKGEVGSP GQPGLPGPKG DAGMPGVDGR PGLEGFPGPQ GPKGDKGSTG EKGERGQDGV
GLPGPPGPPG PPGQIITVSS EDKSLLAFPG PEGRPGHAGF PGPVGPKGDQ GSTGLQGAPG
LKGEKGEPGV IISPDGTVVT AKVKGEKGEP GLRGPVGPSG PPGRAGMKGE IGFPGRPGRP
GMNGLKGEKG DPADVLGSRG LPGPPGPPGP PGPPGSIVYN NGNTFSDSSH PAFPGFHQFQ
GQKGEKGDTG PPGPPGQFPY DASHFGASMR GDKGDAGPKG EKGEPGSTPL YSPGVSGLPG
PPGPQGYPGL PGPKGDSIVG PPGPPGPQGP PGIGYEGRQG PPGPPGPPGP PSFPGPHRQA
VSIPGPPGPP GPPGPPGISG MSLGLRAVPT YQAMLSAAHE LPEGSLVFLT DRQELYVRLR
GGFRRVLLEE QNLIPSSALD NEVYDKPPTL HYAGPQPRGP LHPLRNHVPP ATARPWRGDE
VVANQHRLPE QPLLHHQHEL INGYYVQRRP DPAPVAAHVH QDFQPALHLV ALNTPLSGSM
RGIRGADFQC FQQARQVGLA GTFRAFLSSR LQDLYSIVRR ADRAAVPIVN LQDEVLFNNW
EALFTGSGAP LRAGTRILSF DGRDVLRDAG WPQKSVWHGS DAKGRRLPES YCETWRTEER
AVTGQASSLA SGKLLEQVAS SCQHTFIVLC IENSFMTATK K
//
