ID A0AAQ4RB93_GASAC Unreviewed; 1414 AA.
AC A0AAQ4RB93;
DT 02-OCT-2024, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE SubName: Full=Collagen type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSGACP00000059893.1};
OS Gasterosteus aculeatus aculeatus (three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=481459 {ECO:0000313|Ensembl:ENSGACP00000059893.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000059893.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Benthic {ECO:0000313|Ensembl:ENSGACP00000059893.1,
RC ECO:0000313|Proteomes:UP000007635};
RX PubMed=33598708;
RA Nath S., Shaw D.E., White M.A.;
RT "Improved contiguity of the threespine stickleback genome using long-read
RT sequencing.";
RL G3 (Bethesda) 11:0-0(2021).
RN [2] {ECO:0000313|Ensembl:ENSGACP00000059893.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGACP00000059893.1}
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 RefSeq; XP_040057992.1; XM_040202058.1.
DR Ensembl; ENSGACT00000055997.1; ENSGACP00000059893.1; ENSGACG00000002269.2.
DR GeneID; 120834193; -.
DR KEGG; gat:120834193; -.
DR CTD; 564123; -.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000007635; Chromosome XVI.
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 GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
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; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
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:UP000007635};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1414
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042878011"
FT DOMAIN 117..306
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 76..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..96
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..488
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..541
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..593
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..656
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..673
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..878
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..912
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1023
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1073
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1414 AA; 144918 MW; AC6666067AD3B009 CRC64;
MRTQFGVLFL LTLWVVYSDA WFWPRTGTTT FPPTVDHEGS GSPAFSGEPP SENIAGLGAE
IIGEGQGIQK LVQARDETTD GPRPTTLMPT TLPETQLDSE TGTAVISSHI RQPEDNGVTL
LQLIGNPPPS TIRQVLENDN SPGYVLDHNT NLGQLARAHL PNPFYRNFAL IFNLKPTTDG
AAVIFSVTDG SQKIMYVGVK LSAVQGGNQD VILYYTEPNS EKSYEAARFP VPSMRDTWTR
FAIAVRGDTV MFYLNCDTDP LVMAMERSPD EMELQAGTGV FVGHAGGADP DKFVGVISEL
RVVGDPLAAE RLCEEDEDDS DMASGEGSGS EEPRQPKAPG KKLSTTTPLP PSPPIQQPPL
TRREGDTSTT ETGPKGEKGD RGDPGLKGDR GPIGPKGDAS AGSGSRGGAR GEKGEPGETG
LKGTAGFGYP GMKGDTGPPG PPGSPGPPGP ATEVLVGSGG SVSSRVPGPR GPAGPQGAAG
PQGPPGADGE PGDPGEDGKT GAEGPPGFPG SPGNSGPKGD KGDRGDGQPG PRGPPGPPGP
PGTGSTFVDM EASGFPDLES IRGLPGPPGP PGPPGPATDF VGSASSSGAF GPPGKDGNPG
QPGLPGSDGL PGVSGPKGEK GDSGDLGLPG AVGEKGSRGD PGLPGTPGET GLAGLPGPIG
PVGRPGPPGP PGPGYSVGFD DMEASGEGFR NRLPGERGVE GRQGPPGSPG LQGKDGVPGL
PGQKGTDGLT GRDGRPGLDG FPGPQGPKGD TGNKGERGNP GRDGTGVPGP PGPPGQPGQI
IYQRPDNGGP GLSGQAGLPG PSGPKGDRGD TGPPGYGDKG EKGEPGQVIG PDGNLVHLEG
LTGPKGDRGT PGPVGPPGQY GPAGIKGEMG MPGRPGRPGV NGYKGEKGET GVGYGYPGVP
GQPGPPGPPG PAIPLDRFNR YDDASRNYPA TKGEKGESGD QGPPGIPGTA SNFDIYTLKN
QLKGERGDLG VKGEKGEPGG GGYYDPRFGG AQGPPGPPGK PGLQGPKGES VVGPPGPQGP
PGQPGTGYDG RPGPPGPPGP PGPQGSSSLP GAYRPNYSLS VPGPPGPPGP PGSPARSSGV
TTSRSYDTMI ATARREPEGS LIYILDKADL YLRVRDGVRQ VMLGNYNPFS RDLDNELVEV
QPPPVILYPQ SHDQSHNNGA GHYSQGGSAV RPIEPPPQPP VDRYPPQYDP RFPDTRLTGQ
TDGRSDTQRT ENRHPVTPPR RPSLPVQQPA GPVGPSAPGL HIIALNAPQT GNMRGIRGAD
FLCFQQARAV GLKGTFRAFL SSKLQDLYTI VRRSDRDSTP IVNLKDQVLF SSWESLFGDD
VSKMRENVPI YSFDGRDVVR DSAWPEKMVW HGSSNKGHRQ TDHYCETWRA GDHAVTGLAS
SLQSGRLLQQ TSSSCSGSYV VLCIENAFTS HSKK
//
