ID T1FUF8_HELRO Unreviewed; 1799 AA.
AC T1FUF8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN Name=20212454 {ECO:0000313|EnsemblMetazoa:HelroP192938};
GN ORFNames=HELRODRAFT_192938 {ECO:0000313|EMBL:ESN98469.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP192938, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESN98469.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP192938}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.
CC {ECO:0000256|ARBA:ARBA00006824}.
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DR EMBL; AMQM01005886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB097144; ESN98469.1; -; Genomic_DNA.
DR RefSeq; XP_009023423.1; XM_009025175.1.
DR STRING; 6412.T1FUF8; -.
DR EnsemblMetazoa; HelroT192938; HelroP192938; HelroG192938.
DR GeneID; 20212454; -.
DR KEGG; hro:HELRODRAFT_192938; -.
DR CTD; 20212454; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG1944; Eukaryota.
DR HOGENOM; CLU_000288_18_20_1; -.
DR InParanoid; T1FUF8; -.
DR OrthoDB; 2909504at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0098968; P:neurotransmitter receptor transport postsynaptic membrane to endosome; IBA:GO_Central.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR CDD; cd00992; PDZ_signaling; 4.
DR Gene3D; 2.30.42.10; -; 4.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007248; Mpv17_PMP22.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR23119; DISCS LARGE; 1.
DR PANTHER; PTHR23119:SF44; PROTEIN SCRIBBLE HOMOLOG; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF04117; Mpv17_PMP22; 1.
DR Pfam; PF00595; PDZ; 4.
DR SMART; SM00364; LRR_BAC; 8.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00228; PDZ; 4.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 4.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS50106; PDZ; 4.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1764..1781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 686..774
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 830..919
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1206..1295
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1302..1396
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 442..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1799 AA; 197988 MW; 41A55EFD1A69CB62 CRC64;
MNCIPMWNAC NRQIDYINKQ HAGLIAIPDD ILRYGKTLEE LLLDANQLRE LPKKLFQLTL
LKKLTFSDNQ IIKISSDIGQ LVNLQEIDGS RNELMDIPDT IRHCKELHFV DFSNNPLQKF
PLGFTQLQNL ANLSLNDTSL SMLPNDFGSL TNVEALDFIE NLSNIYCILT NLETLELREN
LLKYLPMSIT SLTKLKLLDL GSNSFEELPE TIGSLVNLEE LLLDSNELSS LPVELGNLKK
LTQLDVSENK LDKLPEQIGN LLNLSDLLLS ENQVEYLPDS IGLLKKLTVL KADQNHLIHL
TTKIGNCSSL QELILIENLI LEIPPTIGKL KYLMVLNVDR NRIQVIPKEI GSCTRLGVFS
IRDNNISLVP QEIGNLRQLK VLDVAGNRLC NLPLALGSCP LKALWLSENQ ATPLLKFQKD
EDDDGEKVLT CFLLPQQRCN VTVNNNNNNK DDNNNNNNDD DHQLRSNNNT LDRETSWADQ
PRLSTVRWDV EEPAASENKS ETHFHRQNTP FPKELRTRHH PHKPHHPPHV MKDSFDRAKN
TESDPLLPAT TTSLRQQQQR NDVTSTTSGI PNVTSSTSGI PSFSLPGTNQ RTKNWINASL
DTTTESNNLL SLDGILNQQK RGFGLANSKT RISSTANETT DSKAIPTFEK LPNSKNKTPQ
NLKSDDDDDD DDVTMTMDGM REERINIHFT RKPGVGLGIS IAGGVGSTPF RGDDEGIFIS
RVTPGGPCHL AGIMVGDKLL EVNGNSLVNA DHHRAVSVLK DAGNDVTAVV ARLVAMENKG
IANQANFLNN NNNNNNNNTV KNERIVNGEK DDDDDDVADE DGGFDWKPIK ATLKKIPGKG
LGFSIVGGRE AAGNRDGDES IYISKITAGG LVDLQTNLKQ GDKLIAINNV DVQSIDHSEV
VNLLMMPANT VEILAHRKAR LPRPSALQQQ QQQQQRNSSF NQQQQQQLLN NNNNNNGNDG
SSRRMRNGSV NNYDDENYLF KPKSKTLLNT SSTSSKMGNN ISPPFSTTTT SITTTTLSNS
FTSNNSNIQK LLTINTSTPP SMFSTKSTTS VVSPVEILFT SSPSYNNPPP TTTSMTSSST
SSSTTAARTS SAPSAAATLA TASLPLKSVK TNGRNFENDV INNGADNNTT SLPKVPKVKK
SSKKSRMNKS GDGDDDDDDD VGGGRNDDDV TIDQSMEDLI LADNSVNHGE KKKTKKKKKD
KHSVETIVIE KNGGPLGMSI VGGVDRICHP FGVLDPGVFI SKVVENGAAS HYNLKIGDRI
LAVNGNSLKE ATHHEAVSSL VSPASEVTLL VQHDPPPPGL QEIKLIKREG EKFGLTIKGG
VDKLGGGNKM GGNPEDDADE GIFISKINPI GVIAKDSRLK VGQRILEVNG ISLLGVTHDD
AVQSLRSIQG GFTLLVCDGY QPKSEKDDEK INNQPLERFY STSSVDRLAG DSFDQQTVVT
KQLKFGSSPA RHATSSSSSH AAAATTATSS SFATKPPQPS SSSSASSSMM VKKKKKKIFS
SAEHLLVDHD LENVPTAATA AAAAADDANA NASSSSPSKR IVKKKKLKVN QSFDTANDSV
NNNYGGINMD SSLIISPSRK KYDHGDDGDD DDDVIKEIKK IKGRKKLLVC RLKRHRLLIT
NTLANGFLLA AGDFVVQQVD RYNEKKLNPE SVREFVDWQR TKRFLITGLC FGPVLHGWYS
LLDWKFPKAT IRSVAWKVFY DQTIACPCSI TYFFFATGLQ EGKRFKECVA ELKEKFVAAY
LVDWLIWPAA QTFNFFFIPP TFRVIFVSST TFVYSIFLSY IKNIELTSEH KWLSAFKIE
//
