ID A0AAQ4S2D2_GASAC Unreviewed; 1309 AA.
AC A0AAQ4S2D2;
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:ENSGACP00000069360.1};
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:ENSGACP00000069360.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000069360.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Benthic {ECO:0000313|Ensembl:ENSGACP00000069360.1,
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:ENSGACP00000069360.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGACP00000069360.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSGACT00000053017.1; ENSGACP00000069360.1; ENSGACG00000002269.2.
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 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:SF1118; LAMININ G DOMAIN-CONTAINING PROTEIN; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1309
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5043051018"
FT DOMAIN 30..219
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 225..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..401
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..506
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..773
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 861..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..918
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..968
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1078
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1309 AA; 133804 MW; 38585147655873AC CRC64;
MRCSFGPELL LCCVLVVLGA AAAQRPEDNG VTLLQLIGNP PPSTIRQVLE NDNSPGYVLD
HNTNLGQLAR AHLPNPFYRN FALIFNLKPT TDGAAVIFSV TDGSQKIMYV GVKLSAVQGG
NQDVILYYTE PNSEKSYEAA RFPVPSMRDT WTRFAIAVRG DTVMFYLNCD TDPLVMAMER
SPDEMELQAG TGVFVGHAGG ADPDKFVGVI SELRVVGDPL AAERLCEEDE DDSDMASGEG
SGSEEPRQPK APGKKLSTTT PLPPSPPIQQ PPLTRREGDT STTETGPKGE KGDRGDPGLK
GDRGPIGPKG DASAGSGSRG GARGEKGEPG ETGLKGTAGF GYPGMKGDTG PPGPPGSPGP
PGPATEVLVG SGGSVSSRVP GPRGPAGPQG AAGPQGPPGA DGEPGDPGED GKTGAEGPPG
FPGSPGNSGP KGDKGDRGDG QPGPRGPPGP PGPPGTGSTF VDMEASGFPD LESIRGLPGP
PGPPGPPGPA TDFVGSASSS GAFGPPGKDG NPGQPGDSGD LGLPGAVGEK GSRGDPGLPG
TPGETGLAGL PGPIGPVGRP GPPGPPGPGY SVGFDDMEAS GEGFRNRLPG ERGVEGRQGP
PGSPGLQGKD GVPGLPGQKG TDGLTGRDGR PGLDGFPGPQ GPKGDTGNKG ERGNPGRDGT
GVPGPPGPPG QPGQIIYQRP DNGGPGLSGQ AGLPGPSGPK GDRGDTGPPG YGDKGEKGEP
GQVIGPDGNL VHLEGLTGPK GDRGTPGPVG PPGQYGPAGI KGEMGMPGRP GRPGVNGYKG
EKGETGVGYG YPGVPGQPGP PGPPGPAIPL DRFNRYDDAS RNYPATKGEK GESGDQGPPG
IPGTASNFDI YTLKNQLKGE RGDLGVKGEK GEPGGGGYYD PRFGGAQGPP GPPGKPGLQG
PKGESVVGPP GPQGPPGQPG TGYDGRPGPP GPPGPPGPQG SSSLPGAYRP NYSLSVPGPP
GPPGPPGSPA RSSGVTTSRS YDTMIATARR EPEGSLIYIL DKADLYLRVR DGVRQVMLGN
YNPFSRDLDN ELVEVQPPPV ILYPQSHDQS HNNGAGHYSQ GGSAVRPIEP PPQPPVDRYP
PQYDPRFPDT RLTGQTDGRS DTQRTENRHP VTPPRRPSLP VQQPAGPVGP SAPGLHIIAL
NAPQTGNMRG IRGADFLCFQ QARAVGLKGT FRAFLSSKLQ DLYTIVRRSD RDSTPIVNLK
DQVLFSSWES LFGDDVSKMR ENVPIYSFDG RDVVRDSAWP EKMVWHGSSN KGHRQTDHYC
ETWRAGDHAV TGLASSLQSG RLLQQTSSSC SGSYVVLCIE NAFTSHSKK
//
