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Database: UniProt
Entry: G3S999_GORGO
LinkDB: G3S999_GORGO
Original site: G3S999_GORGO 
ID   G3S999_GORGO            Unreviewed;      1077 AA.
AC   G3S999;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN   Name=PHKB {ECO:0000313|Ensembl:ENSGGOP00000024664.2};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000024664.2, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000024664.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000024664.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000024664.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC       serine in certain substrates, including troponin I.
CC       {ECO:0000256|RuleBase:RU364123}.
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   -!- 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; CABD030100915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030100916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030100917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030100918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030100919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030100920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030100921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030100922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030100923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030100924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G3S999; -.
DR   Ensembl; ENSGGOT00000023274.2; ENSGGOP00000024664.2; ENSGGOG00000003010.3.
DR   GeneTree; ENSGT00950000183118; -.
DR   HOGENOM; CLU_004177_0_1_1; -.
DR   UniPathway; UPA00163; -.
DR   Proteomes; UP000001519; Chromosome 16.
DR   Bgee; ENSGGOG00000003010; Expressed in adult mammalian kidney and 6 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   InterPro; IPR008928; 6-hairpin_glycosidase_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:SF8; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT BETA; 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|RuleBase:RU364123};
KW   Membrane {ECO:0000256|RuleBase:RU364123};
KW   Prenylation {ECO:0000256|RuleBase:RU364123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT   DOMAIN          33..862
FT                   /note="GH15-like"
FT                   /evidence="ECO:0000259|Pfam:PF00723"
FT   DOMAIN          903..1061
FT                   /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT                   C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19292"
FT   REGION          672..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1077 AA;  123230 MW;  461F025069526F35 CRC64;
     WSRSPDLVIR SVYEPLKSIN LPRPDNETLW DKLDHYYRIV KSTLLLYQSP TTGLFPTKTC
     GGDQKAKIQD SLYCAAGTWA LALAYRRIDD DKGRTHELEH SAIKCMRGIL YCYMRQADKV
     QQFKQDPRPT TCLHSVFNVH TGDELLSYEE YGHLQINAVS LYLLYLVEMI SSGLQIIYNT
     DEVSFIQNLV FCVERVYRVP DFGVWERGSK YNNGSTELHS SSVGLAKAAL EAINGFNLFG
     NQGCSWSVIF VDLDAHNRNR QTLCSLLPRE SRSHNTDAAL LPCISYPAFA LDDEVLFSQT
     LDKVVRKLKG KYGFKRFLRD GYRTSLEDPN RCYYKPAEIK LFDGIECEFP IFFLYMMIDG
     VFRGNPKQVQ EYQDLLTPVL HHTTEGYPVV PKYYYVPADF VEYEKNNPGS QKRFPSNCGR
     DGKLFLWGQA LYIIAKLLTD ELISPKDIDP VQRYVPLKDQ RNVSMRFSNQ GPLENDLVVH
     VALIAESQRL QVFLNTYGIQ TQTPQQVEPI QIWPQQELVK AYLQLGINEK LGLSGRPDRP
     IGCLGTSKIY RILGKTVVCY PIIFDLSDFY MSQDVFLLID DIKNALQFIK QYWKMHGRPL
     FLVLIREDNI RGSRFNPILD MLAALKKGII GGVKVHVDRL QTLISGAVVE QLDFLRISDT
     EELPEFKSFE ELEPPKHSKV KRQSSTPSAP ELGQQPDVNI SEWKDKPTHE ILQKLNDCSC
     LASQAILLGI LLKREGPNFI TKEGTVSDHI ERVYRRAGSQ KLWSVVRRAA SLLSKVVDSL
     APSITNVLVQ GKQVTLGAFG HEEEVISNPL SPRVIQNIIY YKCNTHDERE AVIQQELVIH
     IGWIISNNPE LFSGMLKIRI GWIIHAMEYE LQIRGGDQPA LDLYQLSPSE VKQLLLDILQ
     PQQNGRCWLN RRQIDGSLNR TPTGFYDRVW QILERTPNGI IVAGKHLPQQ PTLSDMTMYE
     MNFSLLVEDT LGNIDQPQYR QIVVELLMVV SIVLERNPEL EFQDKVDLDR LVKEAFNEFQ
     KDQSRLKEIE KQDDMTSFYN TPPLGKRGTC SYLTKAVMNL LLEGEVKPNN DDPCLIS
//
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