ID A0A8C3N5C8_GEOPR Unreviewed; 1688 AA.
AC A0A8C3N5C8; A0A8U8ALI7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 2.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSCPVP00000013821.2};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSCPVP00000013821.2};
OS Geospiza parvula (Small tree-finch) (Camarhynchus parvulus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Thraupidae; Camarhynchus.
OX NCBI_TaxID=87175 {ECO:0000313|Ensembl:ENSCPVP00000013821.2, ECO:0000313|Proteomes:UP000694382};
RN [1] {ECO:0000313|Ensembl:ENSCPVP00000013821.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Enbody D E., Pettersson E M.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCPVP00000013821.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCPVP00000013821.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSCPVT00000014444.2; ENSCPVP00000013821.2; ENSCPVG00000010097.2.
DR Proteomes; UP000694382; Chromosome 7.
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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; 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; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
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:UP000694382};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1688
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5043994763"
FT DOMAIN 381..569
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 37..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..585
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..632
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..843
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..955
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..991
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1285
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1688 AA; 173225 MW; A34D1F0100C2425F CRC64;
MAPPRLGFLL LLACCFSCSE TQLLDWLWDG TKTTGSPALP SEGIPESEPP TSAAAPAPSP
SPGMWGGEVA GNVTTPRQQE PDPATAAPVS EGAAAKTTEQ WDRNATGPVE STAWPSIAPL
HSTSPAPGQQ AASSPTDDPQ LLGTGTHKDP QLLASGTTED LQFLGSGNTE DPQLLWSGTT
KDLQLLETGT TEHLLLLRMR TTEDPQFLGS VTPKDPQLLG SGTTENPQLP RMGTTEDPQS
GATEDLQLLG LGTTEDPQLL GVVSTTDLQL LVAGHTKDPQ PLGTGTTEDP QPLGTGTTKD
AELPGTRTTE NLQLLVMKNT ELLRTVTTEN PELLGNTENP QLLRTVTPED PQFLGTGTPT
METQVSLQRP AGLQPESLSA EISLLELIGD PPTEEIHRIY GPDNNPGYVF GPNANTGQVA
RYHLPSPFYR DFSLLFHIQP TTPRAGVLFA VTDSSQSIIY VGVKLSELRA GQQQIIFYYT
EPGSPSSYPA ATFTVPTLLN QWTRFAISVE EEEVVLYLDC EEYERVRFGR SPDEMELEEG
SGLFVAQAGG ADPDKYQGVI ADLKLRGDPR AAERQCEEEE DDTEVSGDFG SGMDGGQRPS
GKVEGVPGLL DAVPVTSPPV AGGSGPRSGG GSPQQAERTR AEETLRVSTG GAGRKGEKGE
KGERGLKGDS GTSGIVGPGS VKGQKGEKGD LGVKGSAGFG YPGSKGQKGE PGDPGLPGTL
SRHAAGSVVE QVTGPPGTPG KDGAPGRDGE PGDPGEDGKP GEMGPPGFPG MPGEPGLKGE
KGDPGVGPRG PPGPPGPPGP PGPSSKNDKL TFIDMEGSGF AGDLESLRGP RGPPGPPGPP
GVPGLPGEPG RFGMNRTELP GPPGLPGRDG SPGPPGPVGP QGPPGRDGEA GQPGPKGEQG
DMGDLGLPGL PGPKGNKGET GPAGPPGEMG LAGLPGPVGP RGQPGPPGPP GPPGPGYEAG
FGDMEGSGLS FTPGPPGPEG PQGVPGLPGL KGEVGSPGQP GLPGPKGDAG MPGVDGRPGL
EGFPGPQGPK GDKGSTGEKG ERGQDGVGLP GPPGPPGPPG QVISVSGEDQ SLVAFPGPEG
RPGRAGFPGP VGPKGDQGSP GPQGAPGLKG EKGEPGVIIS PDGTVVTAKV KGEKGEPGLQ
GPMGPSGPPG RAGMKGEIGF PGRPGRPGMN GLKGEKGDPA DVLGLRGPPG PPGPPGPPGP
PGSIVYSNGN TFSDSSHPAF PGFHQFSGQK GEKGDTGPPG PPGQFPYDVS HFGTSLRGDK
GDAGPKGQKG EPGSTPLYSP GVSGLPGPPG PQGYPGLPGP KGDSIVGPPG PPGPQGPPGI
GYEGRQGPPG PPGPPGPPSF PGPHRQAVSI PGPPGPPGPP GPPGTGGISL GLQAMPTYQA
MLSAVHELPE GGLVFLTDRQ ELYVRLRGGF RRVLLEEHNL IPSSALDNEV YDKPPTLHYA
GPQPRGPLHP LRNHVPSATA RPWRGDEVVA NQHRLPEQPL LHHQHELING YYIHRRPDPA
PVAAHVHQDF QPALHLVALN TPLSGGMRGI RGADFQCFQQ ARQVGLAGTF RAFLSSRLQD
LYSIVRRADR TAVPIVNLRD EVLFNNWEAL FTGSGAPLRT GARILSFDGR DVLRDAGWPQ
KSVWHGSDAK GRRLPESYCE TWRTEERAVT GQASSLASGK LLEQAASSCQ QAFIVLCIEN
SFMTATKK
//
