SIN1_PONAB
ID SIN1_PONAB Reviewed; 522 AA.
AC Q5RDV5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Target of rapamycin complex 2 subunit MAPKAP1;
DE Short=TORC2 subunit MAPKAP1;
DE AltName: Full=Mitogen-activated protein kinase 2-associated protein 1;
DE AltName: Full=Stress-activated map kinase-interacting protein 1;
DE Short=SAPK-interacting protein 1;
GN Name=MAPKAP1; Synonyms=SIN1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of mTORC2, which regulates cell growth and survival
CC in response to hormonal signals. mTORC2 is activated by growth factors,
CC but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2
CC seems to function upstream of Rho GTPases to regulate the actin
CC cytoskeleton, probably by activating one or more Rho-type guanine
CC nucleotide exchange factors. mTORC2 promotes the serum-induced
CC formation of stress-fibers or F-actin. mTORC2 plays a critical role in
CC AKT1 'Ser-473' phosphorylation, which may facilitate the
CC phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1
CC which is a prerequisite for full activation. mTORC2 regulates the
CC phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the
CC phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is
CC required for complex formation and mTORC2 kinase activity. MAPKAP1
CC inhibits MAP3K2 by preventing its dimerization and autophosphorylation.
CC Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced
CC phosphorylation of ATF2 and ATF2-mediated transcription. Involved in
CC ciliogenesis, regulates cilia length through its interaction with
CC CCDC28B independently of mTORC2 complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 2 (mTORC2)
CC which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary
CC to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-
CC rapamycin. Interacts with ATF2, MAP3K2 and MAPK8. Interacts with GTP-
CC bound HRAS and KRAS. Interacts with IFNAR2, NBN and SGK1. Interacts
CC with CCDC28B (By similarity). {ECO:0000250|UniProtKB:Q9BPZ7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SIN1 family. {ECO:0000305}.
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DR EMBL; CR857789; CAH90052.1; -; mRNA.
DR RefSeq; NP_001124982.1; NM_001131510.1.
DR AlphaFoldDB; Q5RDV5; -.
DR SMR; Q5RDV5; -.
DR STRING; 9601.ENSPPYP00000021975; -.
DR GeneID; 100171855; -.
DR KEGG; pon:100171855; -.
DR CTD; 79109; -.
DR eggNOG; KOG3739; Eukaryota.
DR InParanoid; Q5RDV5; -.
DR OrthoDB; 1492466at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031932; C:TORC2 complex; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR031567; CRIM_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008828; Sin1/Avo1.
DR InterPro; IPR032679; Sin1_N.
DR InterPro; IPR031313; Sin1_PH_dom.
DR PANTHER; PTHR13335; PTHR13335; 1.
DR Pfam; PF16978; CRIM; 1.
DR Pfam; PF05422; SIN1; 1.
DR Pfam; PF16979; SIN1_PH; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cytoplasmic vesicle; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BPZ7"
FT CHAIN 2..522
FT /note="Target of rapamycin complex 2 subunit MAPKAP1"
FT /id="PRO_0000328035"
FT REGION 2..267
FT /note="Interaction with NBN"
FT /evidence="ECO:0000250"
FT REGION 2..184
FT /note="Interaction with MAP3K2"
FT /evidence="ECO:0000250"
FT REGION 468..522
FT /note="Interaction with ATF2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BPZ7"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BPZ7"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BPZ7"
SQ SEQUENCE 522 AA; 59138 MW; 1A9C8E1290573650 CRC64;
MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS GSEIQGSNGE
TQGYVYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ IKCKNIQWKE RNSKQSAQEL
KSLFEKKSLK EKPPISGKQS ILSVRLEQCP LQLNNPFNEY SKFDGKGHVG TTATKKIDVY
LPLHSSQDRL LPMTVVTMAS ARVQDLIGLI CWQYTSEGRE PKLNDNVSAY CLHIAEDDGE
VDTDFPPLDS NEPIHKFGFS TLALVEKYSS PGLTSKESLF VRINAAHGFS LIQVDNTKVT
MKEILLKAVK RRKGSQKVSG PQYRLEKQSE PNVAVDLDST LESQSAWEFC QVRENSSRAD
GVFEEDSQID IATVQDMLSS HHYKSFKVSM IHRLRFTTDV QLGISGDKVE IDPVTNQKAS
TKFWIKQKPI SIDSDLLCAC DLAEEKSPSH AIFKLTYLSN HDYKHLYFES DAATVNEIVL
KVNYILESRA STARADYFAQ KQRKLNRRTS FSFQKEKKSG QQ
