GenomeNet

Database: UniProt
Entry: A0A0D9RQ70_CHLSB
LinkDB: A0A0D9RQ70_CHLSB
Original site: A0A0D9RQ70_CHLSB 
ID   A0A0D9RQ70_CHLSB        Unreviewed;      1235 AA.
AC   A0A0D9RQ70;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN   Name=PHKA2 {ECO:0000313|Ensembl:ENSCSAP00000010759.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000010759.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000010759.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000010759.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC       serine in certain substrates, including troponin I. The alpha chain may
CC       bind calmodulin. {ECO:0000256|ARBA:ARBA00002837}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC       {ECO:0000256|ARBA:ARBA00005131, ECO:0000256|RuleBase:RU364123}.
CC   -!- SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha,
CC       beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB)
CC       are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic
CC       subunit, and delta is calmodulin. {ECO:0000256|ARBA:ARBA00025890,
CC       ECO:0000256|RuleBase:RU364123}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342,
CC       ECO:0000256|RuleBase:RU364123}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342,
CC       ECO:0000256|RuleBase:RU364123}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004423}.
CC   -!- PTM: Although the final Cys may be farnesylated, the terminal
CC       tripeptide is probably not removed, and the C-terminus is not
CC       methylated. {ECO:0000256|PIRSR:PIRSR608734-50}.
CC   -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00007128, ECO:0000256|RuleBase:RU364123}.
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; AQIB01132685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01132686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01132687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01132688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01132689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01132690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007989402.1; XM_007991211.1.
DR   AlphaFoldDB; A0A0D9RQ70; -.
DR   STRING; 60711.ENSCSAP00000010759; -.
DR   Ensembl; ENSCSAT00000012729.1; ENSCSAP00000010759.1; ENSCSAG00000014634.1.
DR   GeneID; 103231681; -.
DR   KEGG; csab:103231681; -.
DR   CTD; 5256; -.
DR   eggNOG; KOG3635; Eukaryota.
DR   GeneTree; ENSGT00950000183118; -.
DR   OMA; QFEHIEC; -.
DR   OrthoDB; 3640971at2759; -.
DR   UniPathway; UPA00163; -.
DR   BioGRID-ORCS; 103231681; 1 hit in 9 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome X.
DR   Bgee; ENSCSAG00000014634; Expressed in liver and 7 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR045583; KPBA/B_C.
DR   InterPro; IPR008734; PHK_A/B_su.
DR   PANTHER; PTHR10749; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10749:SF5; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA, LIVER ISOFORM; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   Pfam; PF19292; KPBB_C; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860,
KW   ECO:0000256|RuleBase:RU364123};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU364123};
KW   Cell membrane {ECO:0000256|RuleBase:RU364123};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600,
KW   ECO:0000256|RuleBase:RU364123};
KW   Lipoprotein {ECO:0000256|PIRSR:PIRSR608734-50,
KW   ECO:0000256|RuleBase:RU364123}; Membrane {ECO:0000256|RuleBase:RU364123};
KW   Prenylation {ECO:0000256|PIRSR:PIRSR608734-50,
KW   ECO:0000256|RuleBase:RU364123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965}.
FT   DOMAIN          8..918
FT                   /note="GH15-like"
FT                   /evidence="ECO:0000259|Pfam:PF00723"
FT   DOMAIN          1063..1207
FT                   /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT                   C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19292"
FT   REGION          974..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1031..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1055
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1232
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608734-50"
SQ   SEQUENCE   1235 AA;  138566 MW;  687972D254A79D82 CRC64;
     MRSRSNSGVR LDGYARLVQQ TILCYQNPVT GLLSASHEQK DAWVRDNIYS ILAVWGLGMA
     YRKNADRDED KAKAYELEQN VVKLMRGLLQ CMMRQVAKVE KFKHTQSTKD SLHAKYNTAT
     CGTVVDDDQW GHLQVDATSL FLLFLAQMTA SGLRIIFTLD EVAFIQNLVF YIEAAYKVAD
     YGMWERGDKT NQGIPELNAS SVGMAKAALE AIDELDLFGA HGGRKSVIHV LPDEVEHCQS
     ILFSMLPRAS TSKEIDAGLL SIISFPAFAV EDVNLVNVTK NEIISKLQGR YGCCRFLRDG
     YKTPREDPNR LHYDPAELKL FENIECEWPV FWTYFIIDGV FSGDAVQVQE YREALEGILI
     RGKNGIRLVP ELYAVPPNKV DEEYKNPHTV DRVPMGKVPH LWGQSLYILS SLLAEGFLAT
     GEIDPLNRRF STSVKPDVVV QVTVLAENNH IKDLLRKHGV NVQSIADIHP IQVQPGRILS
     HIYAKLGRNK NMNLSGRPYR HIGVLGTSKL YVIRNQIFTF TPQFTDQHHF YLALDNEMIV
     EMLRIELAYL CTCWRMTGRP TLTFPISRTM LTNDGSDIHS AVLSTIRKLE DGYFGGARVK
     LGNLSEFLTT SFYTYLTFLD PDCDEKLFDD ASEGTFSPDS DSDLVGYLED TCNQESQDEL
     DQYINHLLQS TSLRSYLPPL CKNTEDCHVF SAIHSTRDIL SVMAKAKGLE VPFVPMTLPT
     KVLSAHRKSL NLVDSPQPLL EKVPESDFQW PRDDHGDVDC EKLVEQLKDC SNLQDQADIL
     YILYVIKGPS WDTNLSGQHR VTVQNLLSEL YGKAGLNQEW GLIRYISGLL RKKVEVLAEA
     CTDLLSHQKQ LTVGLPPEPR EKIISAPLPP EELTKLIYEA SGQDISIAVL TQEIVVYLAM
     YVRAQPSLFV EMLRLRIGLI IQVMATELAR SLNCSGEEAS ESLMNLSPFD MKNLLHHILS
     GKEFGVERSV RPIHSSTSSP AISIHEVGHT GVTKTERSGI NRLRSEMKQM TRRFSADEQF
     FSVGQAVSSS AHSSKSARSS TPSSPTGTSS SDSGGHHIGW GERQGQWLRR RRLDGAINRV
     PVGFYQRVWK ILQKCHGLSI DGYVLPSSTT REMTPHEIKF AVHVESVLNR VPQPEYRQLL
     VEAIMVLTLL SDTEMTSIGG IIHVDQIVQM ASQLFLQDQV SIGAMDTLEK DQTTGICHFF
     YDSAPSGAYG TMTYLTRAVA SHLQELLPNS GCQMQ
//
DBGET integrated database retrieval system