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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//