ID A0A6P9BXR7_PANGU Unreviewed; 777 AA.
AC A0A6P9BXR7;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X1 {ECO:0000313|RefSeq:XP_034272456.1};
GN Name=LOC117665040 {ECO:0000313|RefSeq:XP_034272456.1};
OS Pantherophis guttatus (Corn snake) (Elaphe guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Colubrinae; Pantherophis.
OX NCBI_TaxID=94885 {ECO:0000313|Proteomes:UP001652622, ECO:0000313|RefSeq:XP_034272456.1};
RN [1] {ECO:0000313|RefSeq:XP_034272456.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_034272456.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR RefSeq; XP_034272456.1; XM_034416565.1.
DR AlphaFoldDB; A0A6P9BXR7; -.
DR GeneID; 117665040; -.
DR KEGG; pgut:117665040; -.
DR InParanoid; A0A6P9BXR7; -.
DR OMA; MRADYEC; -.
DR Proteomes; UP001652622; 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 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP001652622};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..777
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028200664"
FT DOMAIN 521..564
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 605..774
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 163..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..290
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..317
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..338
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 81046 MW; 6130028BDBBC2513 CRC64;
METLRGYQPL GFLCLVLLLG GLTPPSVAQF NWWLYSNSKA LTTPAMIPQE AKTDVKQFSV
PTVRSSSIPH NTPDTTAQDA TTEQILDLSS SSGITKEDAF DNSLSVSTFF EGSAMEEDSE
FLSVQTTSKV LTSSVQQSTI TGDSTARPIN VTSQCVCPAI PGLPGPKGAK GDQGPPGKPG
YPGIPGLQGL PGPAGPAGPT GPPGPPGPSG PEGPPGPPGP SGSTLPKILD FTDTKVGEEK
RASIIEGPPG PPGVSGHPGH PGPQGYPGLE GPQGPPGLPG HEGQQGAPGL PGAPGQPGAP
GATGPSGIPG PVGLEGPPGV PGPEGHAGIP GQIGSPGLPG LPGPEGPPGT NGSPGKNGSK
GEKGDRGEPG LPGKPGETGE KGAQGPPGLP GLPGSNQCNS EVGVQGPPGP KGEKGEPGKV
ECSSCKDARS DIDSWVTFIY QKKLKEGVEA NHGPPGPAGK PGPPGPPGPP GVLYINRVYP
VRPRPHCKQP VNQDPCLDSD TELMKDSPDN SQNGYKHATW TFSSKELMLK SASSIPEGSL
VYIIKEAEAF FKTHKGWKKI VMEDSTLLFA ADDPLVSTED NQLDERNIII LTIAPTSIPQ
RIPSLRLVAL NFPLTGNMRG ISGVDLQCHH QAQEANLQGT FRAFLSSDTQ SLSSVVKRTD
RNLPLVNLKG QLLATSWNSL FRRHGISDFN TKEYPIYAFN GLNVMTDPAW INKAVWHGLV
LQINHSKIQD CENWRKASKY LTGQASIPLK DIFLLETSWR CSDRLIVLCV ENSFGST
//
