ID H2P3G5_PONAB Unreviewed; 1749 AA.
AC H2P3G5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000012859.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000012859.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000012859.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR Ensembl; ENSPPYT00000013379.2; ENSPPYP00000012859.2; ENSPPYG00000011521.3.
DR eggNOG; KOG3546; Eukaryota.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000158212; -.
DR HOGENOM; CLU_004003_1_0_1; -.
DR InParanoid; H2P3G5; -.
DR OMA; QDQHQNI; -.
DR TreeFam; TF315821; -.
DR Proteomes; UP000001595; Chromosome 21.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProt.
DR CDD; cd07455; CRD_Collagen_XVIII; 1.
DR CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR035523; Collagen_XVIII_Fz.
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; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1749
FT /note="FZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035317234"
FT DOMAIN 324..441
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 42..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..870
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..912
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..957
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 339..385
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 376..414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1749 AA; 178144 MW; 1A8A03C68DBB3BFA CRC64;
MAPDPRGCRI LLLLFCSLAA ARADLLNLNW LWFNNEDTSH AATTIPEPQG PLPAQPTHMA
PRNGSTEPAT VPGSPEPPSE LLEDGQDTPT SAESPDTPEE NIAGVGAKIL NVAQGIRSFV
QLWNDTVPTE SLTRAETLVL ETPVGPFALP GPSSTPQENG TTLWPSRGTP SSPGAHTTEA
GTLPAPTPSP PSLGRPWAPL TGPSVPPSSS GRASLSSLLG GAPPWGSLQD PDSQGLSPAA
AAASQQLQHP DVRLRTPLLH PLVTGSLGKH AAPSAFSSGL PGALSQVAIT TLIGDSGAWV
SHAANSAGPG LANNSALLRA DPEAPAGRCL PLPPSLPVCG RLGISRSWLP NHLHHESGEQ
VRAGAQAWGG LLRTRCHPFL AWFFCLLLAP PCGSVPPPTP PPCRQFCEAL QDACWSRLGG
GRLPVACASL PTQEDGYCVF IGPAAERVSE EVGLLQLLGD PPPQQVTQTD DPDVGLAYVF
GPDANSGQVA RYHFPSLFFR DFSLLFHIRP ATEGPGVLFA ITDSAQAVVL LGVKLSGVQD
GHQDISLLYT EPGAGQTHTA ASFRLPAFVG QWTHLALSVE GGYVTLYVDC EEFQRMLLAR
SSRGLELEPG AGLFVAQAGG ADPDKFQGMI AELKVRGDPQ VSPMHCLDEE GDDSDGASGD
FGSGLGDARE LLREETGAAL KPRLPMPPPV TTPPLAGGSS TEDSRSKEIE EQTTVASLGG
QTLPGSDSVS TWDGSVRTPG DRVREGGLKG QKGEPGVPGP PGRAGPPGSP CLPGPPGLPC
PVSPLGPAGP ALQPVPGPQG PPGPPGRDGT PGRDGEPGDP GEDGKPGDTG PQGFPGTPGD
VGPKGDKGDP GVGERGPPGP QGPPGPPGPS FRHDKLTFID MEGSGFGGDL EALRGPRGFP
GPPGPPGVPG LPGEPGLFGV NSSDVPGPAG LPGVPGREGP PGFPGLPGPP GPPGREGPPG
RTGQKGSLGE AGAPGHKGSK GDPGPAGARG ESGLAGSPGP AGPPGPPGPP GPPGPGLPAG
FDDMEGSGGP FWSTARSADG PQGPPGLPGL KGDPGMPGLP GAKGEVGADG APGFPGLPGR
EGIAGPQGPK GDRGSQGEKG DPGKDGVGQP GLPGPPGPPG PVVYVSEQDG SVLSVPGPEG
RPGFAGFPGP AGPKGDLGSK GERGSPGPKG EKGEPGSIFR PDGGALGPVQ KGAKGEPGFR
GPPGPYGRPG YKGEIGFPGR PGRPGMNGLK GEKGEPGDAS LGFGMRGMPG PPGPPGPPGP
PGTPVYDSNV FAESSRPGPP GLPGNQGPPG PKGAKGEVGP PGPPGQFPFD FLQLEAEMKG
EKGDRGDAGQ KGERGEPGGG GFFGSRLPGP PGPPGPPGYP GIPGPKGESI RGQPGPPGPQ
GPPGIGYEGR QGPPGPPGPP GPPGPPSFPG PHRQTISVPG PPGPPGPPGP PGTVGASSGV
RLWATRQAML GQVHEVPEGW LIFVAEQEEL YVRVRNGFRK VQLEARTPLP RGTDNEVAAL
QPPVVQLHDS NPYPRREHPH PTARPWRADD ILASPPRLPE PQPYPGAPHH SSYVHLRPAR
PTSPPAHTHR DFQPVLHLVA LNSPLSGSMR GIRGADFQCF QQARAVGLAG TFRAFLSSRL
QDLYSIVRRA DRAAVPIVNL KDELLFPSWE ALFSGSEGPL KPGARIFSFD GKDVLRHPTW
PQKSVWHGSD PNGRRLTESY CETWRTEAPS ATGQASSLLG GRLLGQNAAS CHHAYIVLCI
ENSFMTASK
//