SIP1_YEAS1
ID SIP1_YEAS1 Reviewed; 815 AA.
AC B3LFN4;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=SNF1 protein kinase subunit beta-1;
DE AltName: Full=SNF1-interacting protein 1;
GN Name=SIP1; ORFNames=SCRG_00112;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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=EDV07913.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH408043; EDV07913.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B3LFN4; -.
DR PRIDE; B3LFN4; -.
DR EnsemblFungi; EDV07913; EDV07913; SCRG_00112.
DR HOGENOM; CLU_011585_0_0_1; -.
DR Proteomes; UP000008335; 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_0000377632"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..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 581..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 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; 90958 MW; 02C9A18D603E94BB CRC64;
MGNSPSTQDP SHSTKKEHGH HFHDAFNKDR QGSITSQLFN NRKSTHKRRA SHTSEHNGAI
PPRMQLLASH DPSTDCDGRM SSDTTIDKGP SHLFKKDYSL SSAADVNDTT LANLTLSDDH
DVGAPEEQVK SPSFLSPGPS MATVKRTKSD LDDLSTLNYT MVDETTENER NGKPHHERHR
SSIIALKKNL LESSATASPS PTRSSSVHSA SLPALTKTDS IDIPVRQPYS KKPSIHAYQY
QYLNNDETFS ENSQMDKEGN SDSVDAEAGV LQSEDMVLNQ SLLQNALKKD MQRLSRVNSS
NSMYTAERIS HANNNGNIEN NTRNKGNAGG SNDDFTAPIS ATAKMMMKLY GDKTLMERDL
NKHHNKTKKA QSKKIRSASN SRRSSFASLH SLQSRKSILT NGLNLQPLHP LHPIINDNES
QYSAPQHREI SHHSNSMSSM SSISSTNSTE NTLVVLKWKD DGTVAATTEV FIVSTDIASA
LKEQRELTLD ENASLDSEKQ LNPRIRMVYD DVHKEWFVPD LFLPAGIYRL QFSINGILTH
SNFLPTATDS EGNFVNWFEV LPGYHTIEPF RNEADIDSQV EPTLDEELPK RPELKRFPSS
SRKSSYYSAK GVERPSTPFS DYRGLSRSSS INMRDSFVRL KASSLDLMAE VKPERLVYSN
EIPNLFNIGD GSTISVKGDS DDVHPQEPPS FTHRVVDCNQ DDLFATLQQG GNIDAETAEA
VFLSRYPVPD LPIYLNSSYL NRILNQSNQN SESHERDEGA INHIIPHVNL NHLLTSSIRD
EIISVACTTR YEGKFITQVV YAPCYYKTQK SQISN
