ID S9XP93_CAMFR Unreviewed; 1306 AA.
AC S9XP93;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN ORFNames=CB1_004962001 {ECO:0000313|EMBL:EPY73475.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY73475.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY73475.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
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; KB018702; EPY73475.1; -; Genomic_DNA.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000030684; 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:0004407; F:histone deacetylase activity; IEA:InterPro.
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 Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR045583; KPBA/B_C.
DR InterPro; IPR008734; PHK_A/B_su.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10749; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10749:SF4; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA, SKELETAL MUSCLE ISOFORM; 1.
DR Pfam; PF00723; Glyco_hydro_15; 2.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR Pfam; PF19292; KPBB_C; 2.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 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:EPY73475.1};
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:UP000030684};
KW Transferase {ECO:0000313|EMBL:EPY73475.1}.
FT DOMAIN 8..181
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 237..944
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 1054..1091
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT DOMAIN 1089..1131
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT DOMAIN 1214..1306
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1036..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1212
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR608734-50"
SQ SEQUENCE 1306 AA; 145689 MW; 7C01D5CFC57D0050 CRC64;
MRSRSNSGVR LDGYARLVHQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA
YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTKD SLHAKYNTKT
CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFVQNLVF YIESAYKTAG
FTELRGSRCN AFIPFKLYYT SWPAVIQGSL ASPLQQRVAA VELMIFVPSN SLILAAQTKD
FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS
ILNSILPRAS TSKEVDASLL SVISFPAFAV EDNQLVELTK QEIITKLQGR YGCCRFLRDG
YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGI FSGNAEQVQE YREALEAVLI
KGKNGVPLLP ELYSVPPDKV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG SLMAEGFLAP
GEIDPLNRRF STVPKPDVVV QVSILAETEE IKAILKNKGI DVETIADVHP IRVQPARILS
HIYSSLGCNS RMKLSGRPYR HMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNKMIV
EMLRTDLSYL CSRWRMTGQP TITFPISNSM LDEDGTSLNS SILAALRKMQ DGYFGGARIQ
TGKLSEFLTT SCRTHLSFMD PGPEGKLCSE DYEDYDSELV SGDWMNGYDS ASNARCGDEV
ARYLDHLLAH TDPHPKLAPT SQKGGLNRFR AAVQTTCDLM SLVTKAKELH VQKIHLPRKQ
SGEVDFKALV LQLKETSSLQ EQADILHMLY TMKGPEWDTG LYDEGSATVR ELLTELYGRV
GEIRHWGLIR YISGILRKKV EALDEACTDL LSHQKHLTVG LPPEPREKTI SAPLPYETLT
QLIDEASEGD MSISILTQEI MVYLAMYMRT QPGLFAEMFR LRIGLIIQVM ATELAHSLRC
SAEEATDGLM NLSPSAMKNL LHHILSGKEF GVERSVRPTD SNISPAISIR EVGAVGATKP
ERTGIMQLKS EIKQSPGTSV TLSSDSFPSA YGEQTSKDSR QGQWQRRRRL DGALNRVPVG
FYQKVWKVLQ KMTPGEIKFS VHVESVLNRV PQPEYRQLLV EAILVLTMMA DIEIHSIGSI
IAVEKIVHIA NDLFLQEQKT LGADDIMLAK DPASGICTLL YDSAPSGRFG TMTYLSKAAA
TYVQEFLPHS ICAMQIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDDDH PDSIEYGLGY
DCPATEGIFD YAAAVGGATI TAAQCLIDGV CKVAINWSGG WHHAKK
//
