ID G3H5K2_CRIGR Unreviewed; 1150 AA.
AC G3H5K2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN ORFNames=H671_xg20508 {ECO:0000313|EMBL:ERE65115.1}, I79_005586
GN {ECO:0000313|EMBL:EGV98456.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV98456.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2] {ECO:0000313|EMBL:EGV98456.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000030759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17A/GY {ECO:0000313|Proteomes:UP000030759};
RX PubMed=23929341; DOI=10.1038/nbt.2645;
RA Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA Helk B., Mott J.E., Puhler A., Borth N.;
RT "Chinese hamster genome sequenced from sorted chromosomes.";
RL Nat. Biotechnol. 31:694-695(2013).
RN [4] {ECO:0000313|EMBL:ERE65115.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=17A/GY {ECO:0000313|EMBL:ERE65115.1};
RA Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA Helk B., Mott J.E., Puehler A., Borth N.;
RT "Chinese hamster genome sequenced from sorted chromosomes.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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; JH000161; EGV98456.1; -; Genomic_DNA.
DR EMBL; KE685744; ERE65115.1; -; Genomic_DNA.
DR AlphaFoldDB; G3H5K2; -.
DR STRING; 10029.G3H5K2; -.
DR PaxDb; 10029-XP_007629140-1; -.
DR eggNOG; KOG3635; Eukaryota.
DR InParanoid; G3H5K2; -.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR Proteomes; UP000030759; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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}; Kinase {ECO:0000313|EMBL:EGV98456.1};
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:UP000001075};
KW Transferase {ECO:0000313|EMBL:ERE65115.1}.
FT DOMAIN 8..918
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 1020..1122
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT REGION 636..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1147
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR608734-50"
SQ SEQUENCE 1150 AA; 129188 MW; 03C8454A546E9799 CRC64;
MRSRSNSGVR LDGYARLVQQ TILCYQNPVT GLLSASHDQK DAWVRDNIYS ILAVWGLGMA
YRKNADRDED KAKAYELEQN VVKLMRGLLH CMMRQVDKVE KFKHTQSTKD SLHAKYNTAT
CSTVVGDDQW GHLQVDATSL FLLFLAQMTA SGLRIIFTLD EVAFIQNLVF YIEAAYKVAD
YGMWERGDKT NQGIPELNAS SVGMAKAALE AIDELDLFGA HGGRKSVIHV LPDEVEHCQS
ILFSMLPRAS TSKEIDAGLL SIISFPAFAV EDVNLVNVTK NEIISKLQGR YGCCRFLRDG
YKTPREDPHR LHYDPAELKL FENIECEWPV FWTYLIIDGI FNGDAVQVQE YREALEGILI
RGKDGIHLVP ELYAIPPDKV DEEYKNPHTV DRIPLGKLPH LWGQSLYILS SLLAEGFLAP
GEIDPLNRRF STSVKPDVVV QVAVLAENSH IKRLFRQHGV NVQSIADVHP IRVQPGRILS
HIYAKLGRNK NMKLSGRPYR HIGVLGTSKL YVIRNQIFTF TPQFTDQHHF YLALDNEMIV
EMLRIELAYL CTCWRMTGRP TLTFPVTHTM LTNDGSDIHP AVLSTIRKLE DGYFGGARVK
LGNLAEFLTT SFYTYLTFLD PDCDEKLFDD ISDRSFSPDS ESDLGGYLED SSHPESQDEL
DQYISHLLQS TSLKCYLPPL CKKSEDSHVF SAIHSTRDIL SVMAKAKGLE TPFFPMVLPT
KVLSGHRKSL NLVDSSQTLL KKTPEYDYHW PRDDHGEMDC EKLVGKLKDC SNLQDQADIL
YILYVIKGPS WDTNLFGQHG VTVHSLLSEL YGKAGLNQEW SLIRYISGLL RKKVEVLAEA
CADLLSHQKQ LTVGLPPEPR EKTISTPLPP EELTKLIYEA SGQDISIAVL TQEIVVYLAM
YVRAQPSLFA EMLRLRIGLI IQVMATELAR SLNCSGEEAS ESLMNLSPFD MKNLLHHILS
GKEFGVERSV RPIHSSTSSP AISIHEVGHT GVTKTERSGI TRLRSEMKQC HGLSIDGYVL
PSSTTQEMTA CEIKFAVHVE SVLNRVSQPE YRQLLVEAIM VLTLLSDTEM DRIGGIIHVD
QIVQLANQLF LQDQVSFGAT DILEKDQATG ICHFFYDSAP SGAYGTMTYL TKAVASHLQE
FLPSSGCQMQ
//
