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Database: UniProt
Entry: W5NG59_LEPOC
LinkDB: W5NG59_LEPOC
Original site: W5NG59_LEPOC 
ID   W5NG59_LEPOC            Unreviewed;      1012 AA.
AC   W5NG59;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Protein phosphatase 1 regulatory subunit 3A {ECO:0000313|Ensembl:ENSLOCP00000019618.1};
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:ENSLOCP00000019618.1, 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:ENSLOCP00000019618.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   EMBL; AHAT01021086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NG59; -.
DR   STRING; 7918.ENSLOCP00000019618; -.
DR   Ensembl; ENSLOCT00000019650.1; ENSLOCP00000019618.1; ENSLOCG00000015935.1.
DR   eggNOG; KOG3986; Eukaryota.
DR   GeneTree; ENSGT00940000157682; -.
DR   HOGENOM; CLU_009399_0_0_1; -.
DR   InParanoid; W5NG59; -.
DR   Proteomes; UP000018468; Linkage group LG8.
DR   Bgee; ENSLOCG00000015935; Expressed in muscle tissue and 9 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR   GO; GO:2001069; F:glycogen binding; IBA:GO_Central.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; IBA:GO_Central.
DR   CDD; cd22255; PBD_PPP1R3A; 1.
DR   Gene3D; 2.60.40.2440; Carbohydrate binding type-21 domain; 1.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_sf.
DR   PANTHER; PTHR12307; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR12307:SF2; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 3A; 1.
DR   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        971..999
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..230
FT                   /note="CBM21"
FT                   /evidence="ECO:0000259|PROSITE:PS51159"
FT   REGION          25..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        909..925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1012 AA;  114088 MW;  806E1AD14B758D56 CRC64;
     MESAGQPRQF GASNFLEVID GNSWVEDEDE SPIKPKLSPL PRRKSSVSSD DLEPEPPNVI
     ARKVSFADAF GLDLVSVKEF DTWDVPITSF SDPLEEEAKD IEEYFLSALF TLPSSQYELM
     QKISDQKVEV ESIEFLPGST SIKGIIRVLN LCFQKLVYVR MTLDAWNSFY DLMAEYIPGS
     SDGKTDQFSF KISLVPPYQK EGARIEFCIR YETDVGTFWA NNNGVNYVLF CNKKKVKEAK
     EKQQEESSNK NKKSCLKTNS KDSTTEINDT VVEVGTPGVS QHGAEMTVRE VLETPVPETE
     EHEGDKELET MMDSNFNMTR IEEGRKEVLN PSASEDHCFP EGTETQLGQD SVGQETISIE
     SEDQEPETGT SLFWRSDSSL LVECNGGQTN SEESAHQQLL GSYQAPLLSL QTALNKEGML
     PLKGDEKEAT IKNGNEGENE GEVLQTLIVV EEDLPVCSTE PDESDPQYSL LCLDCLHEKV
     LSSPETLISQ ASLNNEAPSA CKNTLSQEVN ELESKVWEHT ENDVHEGNQR DQRQGSVLSQ
     DEMDVTLDRS ETVNVSLGED DSLDFKNVDP SLYSTEHISK DWKSQSASHK DVEELTHYKI
     QEGKSQDKMI HKVSFTETAG AQQHLVVKAF VAPACQSCQH DNLDPIAEHS PCGRVHSAHT
     QEEEIIFDEP EVTELKQRDL QAKTRQDNKQ PGAAELESII HLSIKQFENT RECDTKQTEH
     AMQHPASETT DQTTSSEEAR AEKEICHNEA QDTYICDKTN GNTPEECESY FSAETETETE
     NVLSEQMAMK MVMIHKRAFL EAVREEKEES GEEDIYADHQ YSFTVDKLES SEQREETSNL
     QSGASLNPFE TAFLRAPVGK AGGTHHTIST KRDRSSAVST FTSRRSEEGA DQRLLQPVLV
     ERQFPLEESE CEQGHDLEED QTQSGETEGH PGMEQPASEI AEDEGRNDLL HWNEEPFILH
     YISKEFFYCS LFILFLVTAY HYDFIACFAL YIFSVYCLCC QGRKQRESFD RK
//
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