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Database: UniProt
Entry: W5MYD7_LEPOC
LinkDB: W5MYD7_LEPOC
Original site: W5MYD7_LEPOC 
ID   W5MYD7_LEPOC            Unreviewed;      1234 AA.
AC   W5MYD7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Protein phosphatase 1 regulatory subunit 9A {ECO:0000313|Ensembl:ENSLOCP00000013396.1};
GN   Name=PPP1R9A {ECO:0000313|Ensembl:ENSLOCP00000013396.1};
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:ENSLOCP00000013396.1, 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:ENSLOCP00000013396.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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DR   EMBL; AHAT01004632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01004633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01004634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015213565.1; XM_015358079.1.
DR   AlphaFoldDB; W5MYD7; -.
DR   Ensembl; ENSLOCT00000013425.1; ENSLOCP00000013396.1; ENSLOCG00000010917.1.
DR   GeneID; 102689540; -.
DR   KEGG; loc:102689540; -.
DR   CTD; 55607; -.
DR   GeneTree; ENSGT00940000155538; -.
DR   HOGENOM; CLU_007401_0_0_1; -.
DR   OrthoDB; 2911512at2759; -.
DR   Proteomes; UP000018468; Linkage group LG11.
DR   Bgee; ENSLOCG00000010917; Expressed in camera-type eye and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd09512; SAM_Neurabin-like; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR040645; Neurabin-1/2_PDZ.
DR   InterPro; IPR043446; Neurabin-like.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR16154; NEURABIN; 1.
DR   PANTHER; PTHR16154:SF22; NEURABIN-1; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF17817; PDZ_5; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   DOMAIN          502..590
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1125..1188
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          1..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..1057
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          598..625
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          678..821
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1182..1219
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        8..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..838
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..856
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..979
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1034
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1234 AA;  136070 MW;  EC46BE9163008BAE CRC64;
     MMKTEASGER STLRSASPHR NAYRTEFQAL KNAFDQPRRD GDPKPKEACE KPPQARGRQY
     GSNVNRIKNM FMQMGMGPNE NTGPPSKTKG KEGSSPQKIR RPKPSVDKTG ESAVKLQATV
     SERVSRFDTS RDGTAHSKFS ETRKMFEQTI RETSQSSRSS SGKDRKGSHE HLDEWKGMRS
     NLGSTDSLDS LCSRTEASSP TVSQLSAVFE NADQQNAAAW KKTGSKGLCS PDGSQRQTEL
     SEDDVSWQQS PPHRRHKRHG QKQAIPLSSS SEDLLSPSPV SETADEGKGI SSVSQQRNEH
     EKEMEYNQGN AEDFRADAAS DCGVQRQMGA VAGSEVDGVY SDSAVSEPSA GNEHRTQIPK
     MPPSQLNEQA EGPVLADSAW VSDEHAKDPS EGYTGSEKAI GTSESAMYYQ GWGESCTDPE
     DQACSEENSH YEPDSEIVEI PGLPEEEDVA SNRKIRFSTA PIMVFKTYSN EDYDRRNDEV
     DPVAASAEYE LEKRVEKLDL FPVDLEKDED GLGISIIGMG VGADAGLEKL GIFVKTVIEG
     GAAQKDGRIK VNDQIVEVDS ISLVGVTQNF AATVLRNTEG VVRFLIGREQ PGQVSEVAQL
     ISQTLEQERR QREMLEQHYV QYDADDDETG QYATDDEDED MVPDITGGDM AIEVFDLPET
     ADMFSPTEMD ATKLSHKFRE LQIKHAVTEA EIQKLKSKLQ STENERVRWE REKTQLQKSI
     DDNKERMLKL EGYWIEAQTL CHTVNEHLKD TQSQYQALEK KYNKAKKLIK DFQQKELDFV
     KREQVEKRKF EDAEKVHLIE IQGLQAQISN LEAELLNLMK QSGTQVNNNN NSAERISTLG
     REEPSESTED ALRTRGAVAD GDFAEAVPET ERLDSEALKA RAQLSVKSRR GRPSRPRPRG
     SLSSTDGEDG LERKTAEGGS SPLHSSMPAL PSSPKPTSRA LDPGTSSSPP AQGGGASTAV
     LEDSPTSSPS RSCSSEASPL HHPQLDREDE GSLSPLISSP SVGPLGKTKR KLIDLGSPAR
     HSPGREKKDK DSSRLSSGNS STEPSSENSP EKHKAKNVGL NNDVSASSVS SADFSGLVAE
     PKITGRSHSL ALSSDESLEM IDDEILDDSH SPKHQQWQNR AVLEWSCQQV SHWLMGLNLE
     QYVPEFTAKG INGEQLLQLD GRKLKSLGVV SSQDRALIKK KLKDLRAVVD KALKTREKLE
     KHREKLWKKE QELLQREAKK TGKTSGGPAE GSAE
//
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