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SIP1_YEAS7
ID   SIP1_YEAS7              Reviewed;         815 AA.
AC   A6ZZ19;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=SNF1 protein kinase subunit beta-1;
DE   AltName: Full=SNF1-interacting protein 1;
GN   Name=SIP1; ORFNames=SCY_1307;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Beta subunit of the SNF1 kinase complex, which is required
CC       for transcriptional, metabolic, and developmental adaptations in
CC       response to glucose limitation. Has a structural role, mediating
CC       heterotrimer formation, and a regulatory role, defining carbon source-
CC       regulated subcellular location and substrate specificity of the SNF1
CC       kinase complex. Promotes the PKA-regulated relocalization of the SNF1
CC       kinase complex to the vacuolar membrane in response to various types of
CC       carbon stress (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SNF1 kinase complex, a heterotrimeric complex
CC       composed of the catalytic alpha subunit SNF1, one of the three related
CC       beta subunits SIP1, SIP2 or GAL83, and the regulatory gamma subunit
CC       SNF4. The beta subunit serves as a bridge between the catalytic and the
CC       regulatory subunit. Interacts (via KIS domain) with SNF1. Interacts
CC       (via ASC domain) with SNF4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Vacuole membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Resides in the cytosol during growth in
CC       glucose and relocalizes to the vacuolar membrane in response to carbon
CC       stress. {ECO:0000250}.
CC   -!- PTM: Phosphorylated by SNF1 in vitro. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN60749.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAFW02000145; EDN60749.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A6ZZ19; -.
DR   PRIDE; A6ZZ19; -.
DR   EnsemblFungi; EDN60749; EDN60749; SCY_1307.
DR   HOGENOM; CLU_011585_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0043254; P:regulation of protein-containing complex assembly; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR032640; AMPK1_CBM.
DR   InterPro; IPR006828; ASC_dom.
DR   InterPro; IPR037256; ASC_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR030073; Sip1.
DR   PANTHER; PTHR10343:SF87; PTHR10343:SF87; 1.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   Pfam; PF04739; AMPKBI; 1.
DR   SMART; SM01010; AMPKBI; 1.
DR   SUPFAM; SSF160219; SSF160219; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipoprotein; Membrane; Myristate; Phosphoprotein; Vacuole.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..815
FT                   /note="SNF1 protein kinase subunit beta-1"
FT                   /id="PRO_0000377633"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..716
FT                   /note="Kinase-interacting sequence (KIS); required for
FT                   interaction with SNF1"
FT                   /evidence="ECO:0000250"
FT   REGION          583..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..804
FT                   /note="Association with SNF1 kinase complex (ASC) domain;
FT                   required for interaction with SNF4"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         331
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         494
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         497
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   MOD_RES         643
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32578"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   815 AA;  91054 MW;  2D6812DBC9DE1B31 CRC64;
     MGNSPSTQDP SHSTKKEHGH HFHDAFNKDR QGSITSQLFN NRKSTHKRRA SHTSEHNGAI
     PPRMQLLASH DPSTDCDGRM SSDTTIDKGP SHLFKKDYSL SSAADVNDTT LANLTLSDDH
     DVGAPEEQVK SPSFLSPGPS MATVKQTKSD LDDLSTLNYT MVDETTENER NDKPHHERHR
     SSIIALKKNL LESSATASPS PTRSSSVHSA SLPALTKTDS IDIPVRQPYS KKPSIHAYQY
     QYLNNDETFS ENSQMDKEGN SDSVDAEAGV LQSEDMVLNQ SLLQNALKKD MQRLSRVNSS
     NSMYTTERIS HANNNGNIEN NTRNKGNAGG SNDDFTAPIS ATAKMMMKLY GDKTLMERDL
     NKHQNKTKKA QNKKIRSASN SRRSSFASLH SLQSRKSILT NGLNLQPLHP LHPIINDNES
     QYSAPQHREI SHHSNSMSSM SSISSTNSTE NTLVVLKWKD DGTVAATTEV FIVSTDIASA
     LKEQRELTLD ENASLDSEKQ LNPRIRMVYD DVHKEWFVPD LFLPAGIYRL QFSINGILTH
     SNFLPTATDS EGNFVNWFEV LPGYHTIEPF RNEADMDSQV EPTLDEELPK RPELKRFPSS
     SRKSSYYSAK GVERPSTPFS DYRGLSRSSS INMRDSFVRL KASSLDLMAE VKPERLVYSN
     EIPNLFNIGD GSTISVKGDS DDVHPQEPPS FTHRVVDCNQ DDLFATLQQG GNIDAETAEA
     VFLSRYPVPD LPIYLNSSYL NRILNQSNQN SESHERDEGA INHIIPHVNL NHLLTSSIRD
     EIISVACTTR YEGKFITQVV YAPCYYKTQK SQISN
 
 
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