ID A0AA35PLI3_9SAUR Unreviewed; 808 AA.
AC A0AA35PLI3;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X1 {ECO:0000313|EMBL:CAI5790300.1};
GN ORFNames=PODLI_1B009726 {ECO:0000313|EMBL:CAI5790300.1};
OS Podarcis lilfordi (Lilford's wall lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=74358 {ECO:0000313|EMBL:CAI5790300.1, ECO:0000313|Proteomes:UP001178461};
RN [1] {ECO:0000313|EMBL:CAI5790300.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T., Gomez Garrido J.;
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR EMBL; OX395138; CAI5790300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA35PLI3; -.
DR Proteomes; UP001178461; Chromosome 13.
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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; IPR016187; CTDL_fold.
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; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:CAI5790300.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP001178461};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 556..599
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 641..808
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 77..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..237
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..357
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..504
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 84255 MW; 286BA62765CB9E6B CRC64;
MVLSTPTLWD TPGTFTEEVA VSSEATTPGL ATSAADKEEV FPGMDFPFQN ILEGSTEDED
DEFLHSLVTA PGNEVSTELE DAKPSMSSVH QTTIRGDSET KEAQPVTEKS WWPPATVTKE
HPQKAEEDPH VSTPDVHQTV GRGDSVAKEE EPQLLTPSVH QTVVRGDSVA KEVITKEETS
SISPPKTAAA SIIGMHNLSQ CVCPATPGPR GAKGDKGDQG PPGERGLPGE RGLAGNPGQP
GPAGPPGPPG QSLPGSPECG DANGGNEKGV SIMEGPPGPM GYPGLPGPPG YPGQEGPQGP
PGLPGHEGQQ GTPGLPGTPG QPGPPGSTGP AGMPGPVGAE GIPGAMGPEG HPGLPGHMGP
PGPPGTPGQK GPPGREGLPG KDGPKGEKGE VGLQGPPGNP GVKGEMGLQG VPGPMGPPGE
NQCNTHARVL GPPGPKGEKG EPGERDCCNC PRATKADSDS WTPFTYQENG KGDLEIYGSI
ASRGPPGPAG NPGMPGPPGP PGPPGVIYLN RVIPIPPRRH CKQPLSQDPS LDSDDGLSLK
DSSNENQYGF KHSTWIFKSK ELMFKSASSI PEGSLVYVSE GNEAFFRTPK GWSRLLLEDS
ESLLVGDDPL VSTDRNQVQN DKSQATVQTV PPSIPQRIPS LRLVALNIPL TGSMNGIGGV
DLRCYRQSQE AKLRGTFRAF LSSSTQSLVS IVKRTDRNLP IVNLKGQLLA KSWNSLFSSA
ARFNSPKSPI YTFNGRNVMT DPMWRQKAVW HGVKQLGGQA ENQDCQEWRT ASSQSKGLAS
PPAGGKFLTV DTHSCSDFLI VLCVENAF
//
