ID W5N6R5_LEPOC Unreviewed; 2193 AA.
AC W5N6R5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Multiple PDZ domain crumbs cell polarity complex component {ECO:0000313|Ensembl:ENSLOCP00000016324.1};
GN Name=MPDZ {ECO:0000313|Ensembl:ENSLOCP00000016324.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016324.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016324.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR EMBL; AHAT01002021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01002022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015201288.1; XM_015345802.1.
DR STRING; 7918.ENSLOCP00000016324; -.
DR Ensembl; ENSLOCT00000016354.1; ENSLOCP00000016324.1; ENSLOCG00000013247.1.
DR GeneID; 102683920; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000155586; -.
DR InParanoid; W5N6R5; -.
DR OMA; HMSHADS; -.
DR OrthoDB; 2911488at2759; -.
DR Proteomes; UP000018468; Linkage group LG4.
DR Bgee; ENSLOCG00000013247; Expressed in testis and 12 other cell types or tissues.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0120192; P:tight junction assembly; IBA:GO_Central.
DR CDD; cd00992; PDZ_signaling; 13.
DR Gene3D; 2.30.42.10; -; 13.
DR Gene3D; 1.10.287.650; L27 domain; 1.
DR InterPro; IPR015132; L27_2.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR032078; MPDZ_u10.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR19964; MULTIPLE PDZ DOMAIN PROTEIN; 1.
DR PANTHER; PTHR19964:SF10; MULTIPLE PDZ DOMAIN PROTEIN; 1.
DR Pfam; PF09045; L27_2; 1.
DR Pfam; PF16667; MPDZ_u10; 1.
DR Pfam; PF00595; PDZ; 13.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 13.
DR SUPFAM; SSF101288; L27 domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 13.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 13.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 3..63
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 140..227
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 260..340
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 374..460
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 551..632
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 697..772
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1044..1112
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1198..1290
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1482..1565
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1609..1690
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1752..1835
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1848..1930
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1987..2073
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 2110..2193
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 491..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2193 AA; 235937 MW; 8C018AB5728CD7AF CRC64;
MIETIDTQRA LQAVERLQAK LKERGDVLTE EKLNMLKTVL QSPLFQQILT LQTSVQQLKE
QVDAGPASLS PNTELPQTIK PGLCSLPLSD SYVLAQQNGN YGIQRDTPAL SITPQINGKP
SVDEFEHLIR SMAQGRYVMH IELVKPISGG LGFSVVGLKS ENRGELGIFV QEIQPGSVTH
CDGKLKEGDQ ILSINGQPLD QTITHQEAIS ILQKASEKVN LIVARGPIPQ LASPVVSRTP
SAASTLSAHS SATHWQHMET IELVNDGTGL GFGIVGGKST GVIVKTILQG GVADQDGRLR
SGDHILKIGD TDLHGMGSEQ VAQVLRQCGN RVKLVITRGA IEDSSAPPAP VLPPVVELQC
EMTDYEEDDI DAFDVELTKN AQGLGITIAG YVGDKTSEPS GIFVKSITKG SAVEQDGRIH
IGDQIIAVDG TNIQGFTNQQ AVEVLRHTGQ TVHLKLMRRG FRPEEPLISE HKPLPKVVKE
LAVDRMDSDI TIEDSDRKQK PYPSICGSSS ITPTEDEQIQ SKEGTLLTAV EEEELKKKWQ
SLLGPSNEVV VAQVEKFSES SGLGISLEAS SGHHYIRSVL PEGPVGRSGR LFSGDELLEV
NGISLIGENH KEVISILKEL PVFVTLVCCR PALLLDSDSD IGGKNGLQEH FDEPEQKVHL
DLGDCVGSSE TDDIVKENVT EETLGSSLAM WETEIQDIEL EKGDMGLGFS ILDYQDPVDP
EKTVIVIRSL VPDGVAEVDG RLLPGDRLMF VNDTNLENAS LEDAVQALKG APVGKVRIGV
AKPLPPTPEE GCSSAKDDSI FYTAQQFEDE EQADAAVFHA ELAMIDSNEA DLTDEKTFDS
QYPGEEDDTF QESMLALHGS TCSVDLDYQL SMHSSTPKST YEDAFAKPSF SAATEFADEA
EPFFPEEKRI TLFQPWKATS SALPFGATNK TPSPEQHINL METDCVMPEV VQSEPCSALN
HDKRSIQSFE TEMELDKASD ACAEYKPCHE GSVSTDPGRE DTDDRSSHQE GFVPVKRNED
MEDQGLVENI DNEMFSSGSS FERTITVVKG NSSLGMTVSA VKDGSGMIIR SIIHGGSISR
DGRLAVGDCI LAINGEPTTN LTNAQARAML RRHSLIGPDI RSSCAPADDQ SPFYVITYVP
SEYLEEYRIS LVHLKDETTS GAPSTCAEAG ELPEREDGEG EESEMQSSAY SNWNQPRKVE
LFREAGKSLG ISIVGGRGMG SRLNNGEVMR GIFIKHILED SPAGRNGTLK TGDRIVEVDG
IDLRDASHEQ AVEAIRKAGN PVVFMVQSIV HRPRPDSFYS PSSSPVIEKH ITTMPLPHQL
CKKPPLPFLL PKPIPEPAFS STNPFVASFQ PSLFQTMTTE SNEEKCIPTS NVIAKHEIKI
KGSESHSRLF LRLSPTNPFA PTPFKAPSNR LDLEAGKVSL SVPLVSSLPV VPPIGETETD
TLMEPENLAL PMDSPDEEED EFGYSWKKII QRYGSLPGVL HMIELEKGKT GLGLSLAGNK
DRSRMSVFVV GIDPSGAAGR DGRILVGDEL LEINGQILYG RSHQNASSII KSAPSKVKII
FIRNTDALNQ MAAGPVKECG DMLESQTELD MCAVSPSAID FDLFKNIQHI ILPKDQGGLG
IAISEEDTSG GVVIKSLTDN GAAGKDGRIK VNDKILAVDD ETVVGCPVEK VINLLKRSKS
TVKLTICSED LSSLSSCVNL PESASDVKIS QSLPTAFISD VDPFKNASRS STPATMASDP
VTCPIIPGCE TTIDISKGRT GLGLSIVGGS DTLLGAIIIH EVYEEGAASK DGRLWAGDQI
LEVNGIDLRN ATHDEAINVL RQTPQKVRLT VYRDEAQYKE DDMWDVFFLE LQKKPGEGLG
LSIVGKRNDT GVFVSDIVKG GIADTDGRLM QGDQILSVNG EDVRSATQES VAALLKCCIG
TITLEVGRYK AGPFHSERRL SHSSQVSETG SFGASSCLSG SGSGLGDNFE SRRKSLDSGS
DFQELRTVEF TKGPLDSLGI SIAGGVGSPL GDIPIFIAMM HPTGLAAQTQ KLKIGDRIVS
ICGTSTEGMS HSQAVTLLKN ASGTIGLQVC AGGDASVTGS SHEQTASLSL SGLTASSIFH
DDLGPPQYKT ITLDRGHDGL GFSIVGGFGS PHGDLPIYVK TVFVKGAASE DGRLKRGDQI
IAVNGQSLEG VTHEEAVAIL KRTKGTVNLT VLS
//