ID A0A9F2WEF8_PYTBI Unreviewed; 1210 AA.
AC A0A9F2WEF8;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_007439697.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_007439697.1};
OS Python bivittatus (Burmese python) (Python molurus bivittatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Henophidia; Pythonidae; Python.
OX NCBI_TaxID=176946 {ECO:0000313|Proteomes:UP000695026, ECO:0000313|RefSeq:XP_007439697.1};
RN [1] {ECO:0000313|RefSeq:XP_007439697.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_007439697.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR RefSeq; XP_007439697.1; XM_007439635.3.
DR AlphaFoldDB; A0A9F2WEF8; -.
DR GeneID; 103058183; -.
DR KEGG; pbi:103058183; -.
DR CTD; 80781; -.
DR OMA; VQDQHQN; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000695026; Unplaced.
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 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 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; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 4.
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,
KW ECO:0000313|RefSeq:XP_007439697.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000695026};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 875..922
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 1036..1205
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 64..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..264
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..370
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..431
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..520
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..843
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 122678 MW; 6E9F5B92B0E9EAE9 CRC64;
MDCEEFKTVH LERSPDEMEL EEGSGLFVAQ AGGADPDKYQ GVIAELKIKG NPWAAGVQCV
EEEDDCDTMC GDSGSGIDIK QSSSEKESVI PVLSSLPVPP PVTSPPTAKK PVQPEDSLSL
QTEHTESKER PPFVSTAGTK GEKGDPGEKG QRGPKGDPGP GILSTNGDKG EKGSAGFGYP
GSKGQKGEPG IPGLPGPVGP PGPSGTVIQH PDGSTVEQVP GQPGAMGPPG SPGKDGQPGK
DGEPGDPGED GKPGDVGPQG FPGTPGEPGP KGEKGEPGVG ARGPPGPPGP PGQPALNSKL
DKLTFLDMEG SGFGSELETL RGPRGPPGPP GPPGVPGLPG QPGRFGTNGT DFPGLPGLPG
VPGRDGSSGI PGPPGPPGLP GRDGIPGQPG ETGARGESGE VGFPGAPGPK GSKGEPGPPG
APGETGLAGL PGPMGPRGLP GPPGPGIAAE FIDMEGSGVP FVSGGPGIRG PEGPPGLPGL
PGLPGPPGPK GYEGIIGLPG LPGEKGNPGL PGLDGRPGLE GFPGPQGPKG DQGDPGPQGE
KGQDGIGLPG SPGLPGPPGQ VVYLSNEDKT LPVLPGPEGP VGPKGDPGSP GLQGYPGLKG
EKGDPGVTGP DGTILAAEAK GEKGEPGPRG PVGPAGPPGR SGQNGEIGFP GRPGRPGMNG
LKGEKGDPAD LSGGLGLRGL PGPPGPPGPP GLPGSPGSAV PVYENNAFGD LGPPGPPGLP
GYHGTPGQKG EKGEEGPPGP PGQFPYDLSR LSSTFRGERG DKGDPGLKGE KGEPGGGELL
GSSVAGLPGP PGYPGLPGPK GESIRGPPGP PGPQGPPGAG FEGRPGLQGP PGPPGPPGPP
SFPGPHRQHI SIPGPPGPPG PPGPPGVSDP SSLGVRILAT YQSMMSRAHE VPEGQLLFIR
EREELYIRVH NGFRKILLEE RISIPGSGLD NEVYDRSSSI HYSHGDTASS GSQRPFQPHS
PVHAHREHST YSTAKPWRGD ESIVNSHHLP EQPAIHQPHQ GAQSQQGSLD HFFPNHRQTE
TAPLAVHTHH AFQPALHLIA LNAPQSGSMR GIRGADFQCF QQARQVGLSG TFRAFLSSRL
QDLYSIVRRA DRSTVPIVNL RDEVLFNNWE NLFSGSEAPF RTGVRILSFD GRDVLRDSAW
PQKYVWHGSD TKGRRLTESY CETWRTDDTV VTGQASSLAS GKLLEQKSNS CRNAFVVLCI
ENSFMTSSKK
//
