ID A0AAD8G6P8_ACIOX Unreviewed; 1669 AA.
AC A0AAD8G6P8;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=AOXY_G14088 {ECO:0000313|EMBL:KAK1165527.1};
OS Acipenser oxyrinchus oxyrinchus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=40147 {ECO:0000313|EMBL:KAK1165527.1, ECO:0000313|Proteomes:UP001230051};
RN [1] {ECO:0000313|EMBL:KAK1165527.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=STURGEONOMICS-FGT-2020 {ECO:0000313|EMBL:KAK1165527.1};
RC TISSUE=Whole blood {ECO:0000313|EMBL:KAK1165527.1};
RA Stock M., Klopp C., Guiguen Y., Cabau C., Parinello H.,
RA Santidrian Yebra-Pimentel E., Kuhl H., Dirks R.P., Guessner J., Wuertz S.,
RA Du K., Schartl M.;
RT "Atlantic sturgeon de novo genome assembly.";
RL Submitted (FEB-2022) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK1165527.1}.
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DR EMBL; JAGXEW010000012; KAK1165527.1; -; Genomic_DNA.
DR Proteomes; UP001230051; Unassembled WGS sequence.
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; IPR010363; DUF959_COL18_N.
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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 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 PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP001230051};
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..1669
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042080818"
FT DOMAIN 306..494
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 355..493
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 76..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..666
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..795
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..844
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..902
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..951
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1126
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1326
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1669 AA; 171840 MW; BF5F4474AAB144DC CRC64;
MAKSGNMLGC SLVLLACVSY SDAQWGWWPF GKDAQATTQT TATQENQGLQ STANEATGLE
TTMVIPQAHQ EGHGLLSVST RSPDSEAASP TTGPPPPGRV TEENLAGVGA QILNVAEGIL
SFVQTWDQKP TAETKDGAVE VSTSPAEDRE TTTDGHKTDR GTTLPIARQV TEQPKAKANS
LPVTKPWVER LLLENGTTTL HTKSVLENLP DVNLESSGEG ESGSSMGDRQ FEAGQLEMGN
LTSSFSSIRS GELLQVGNTS DWRDSVTNES LHGGTGFLKM QLSDNLTDFA NWTTAGNDTS
NRDDVGVSLL QLIGDPPPEE ITKIYGPDNS PGYVFGPDAN TGQLARAHLP SPFYRDFSLL
FHLQPTTPKA GVIFSVTDPT QASMYVGVKL SAVQAGKQKV LFYYTEPGSQ TSYQAAAFNV
PSLANRWTRF AISVEGEEVF FFLDCEESEA TRFERSPDEM ELESGAGVFV GQAGGADPDR
FVGVIAELRV VGDPRAAERH CDEEGDDSDG ASGDFGSGYE ERPKIETVTP PAQRPLKQPP
VTAPSTGRKE KLSPQTNAET AGKQIVDSQT HSEVKSQPGV PGQAGKLQKS DTMGPAGPTG
PKGERGEKGD QGERGPQGAK GESVGAAGGA AGPRGEKGSA GFGYPGKKGD KGDPGPPGPP
GPPSPPAERL ERGDGSVVEQ IVGARGPPGP AGPPGPSGAD GEPGDPGEDG IAGPAGPPGF
PGTPGDPGQK GEKGDPGEGK PGPRGPPGLP GPAASRSETF FDMEGSGFPD LDSIRGPQGL
PGIPGPPGPP GPPAAPNLSS GRQASIGPPG PRGIDGKDGI PGVQGPPGPP GPPGNNGQPG
LVGPRGEKGD AGDLGLPGAV GEKGSKGDVG PPGISGQTGL AGLPGPMGPV GQPGPPGPPG
PGFPVGFDDM EGSATGSIHG PGVRGPDGRP GVPGPPGLPG IPGNNGLPGL PGAKGEAGSP
GFSGVDGQPG LDGFPGLKGP KGDRGDRGER GEQGRDGVGI PGQPGLPGPP GRIIYQPDNR
EGNIAPGREG IQGPPGQAGF PGPRGPKGDR GDSGQPGYGI KGEKGEPAAI IGPDGNILSS
AFLGGFGGEK GDPGIPGPVG PVGPYGRPGH KGEIGLPGRP GRPGINGFKG EKGEPSDVHS
GYAVIGPPGP RPPAPGPPGQ LTERYDFNEA VPRYPGLPGP KGERGFPGYT GEKGEQGQPG
LPGQPGGLPD FDIYALKREL KGEQGDKGPQ GEKGEPGGGY YDPRYSAPQA PPGQPGSPGL
PGPKGDSIRG PPGPQGPPGT PGVGYDGRPG QPGPPGPPGP PYAAGASRQS ISIPGPPGPQ
GPPGPPGHSS GVTILRTYQT MVTTARGLPE GTMIFVLDKA DIYIRVRDGF RQVLLGDYTP
FFGGGVLENE VAAVQPPPVV HYSQGHSPNS GAGHISHNEP VNRQPEQKPH WPHPPHQPDQ
GHVVYPSTPE RQPAGRNPAK PEFSYPSYPS PPQRRPSQPE NTQPAGHEHG TGPALHLIAL
NAPQTGDMRG IRGADFQCFQ QARAVGLTGT FRAFLSSKLQ DLYSIVRRAD RATLPIINLR
DEVLFDNWES LFDGSDAQMK PNVAVYSFDG RDVLRDSTWH EKMVWHGSNN KGHRVTDNYC
ETWRTGDRAV TGLASSLQAG RLLQQRPSSC TSSHIVLCIE NSYILQSKK
//
