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}.
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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
//