ID   MOB1A_PONAB             Reviewed;         216 AA.
AC   Q5RAE0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=MOB kinase activator 1A;
DE   AltName: Full=Mob1 homolog 1B;
DE   AltName: Full=Mps one binder kinase activator-like 1B;
GN   Name=MOB1A; Synonyms=MOBK1B, MOBKL1B;
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, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activator of LATS1/2 in the Hippo signaling pathway which
CC       plays a pivotal role in organ size control and tumor suppression by
CC       restricting proliferation and promoting apoptosis. The core of this
CC       pathway is composed of a kinase cascade wherein STK3/MST2 and
CC       STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates
CC       and activates LATS1/2 in complex with its regulatory protein MOB1,
CC       which in turn phosphorylates and inactivates YAP1 oncoprotein and
CC       WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its
CC       translocation into the nucleus to regulate cellular genes important for
CC       cell proliferation, cell death, and cell migration. Stimulates the
CC       kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2
CC       to activate STK38 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds STK38 and STK38L. Interacts with LATS1 and LATS2 (By
CC       similarity). Forms a tripartite complex with STK38 and STK3/MST2 (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated by STK3/MST2 and STK4/MST1 and this phosphorylation
CC       enhances its binding to LATS1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR   EMBL; CR859077; CAH91270.1; -; mRNA.
DR   EMBL; CR859538; CAH91704.1; -; mRNA.
DR   RefSeq; NP_001125752.1; NM_001132280.1.
DR   AlphaFoldDB; Q5RAE0; -.
DR   SMR; Q5RAE0; -.
DR   STRING; 9601.ENSPPYP00000013698; -.
DR   Ensembl; ENSPPYT00000053329; ENSPPYP00000041432; ENSPPYG00000012284.
DR   GeneID; 100172677; -.
DR   KEGG; pon:100172677; -.
DR   CTD; 55233; -.
DR   eggNOG; KOG0440; Eukaryota.
DR   GeneTree; ENSGT01050000244898; -.
DR   HOGENOM; CLU_038321_3_1_1; -.
DR   InParanoid; Q5RAE0; -.
DR   OMA; TCEVMSA; -.
DR   OrthoDB; 1127941at2759; -.
DR   TreeFam; TF300789; -.
DR   Proteomes; UP000001595; Chromosome 2A.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035329; P:hippo signaling; IEA:Ensembl.
DR   Gene3D; 1.20.140.30; -; 1.
DR   InterPro; IPR005301; MOB_kinase_act_fam.
DR   InterPro; IPR036703; MOB_kinase_act_sf.
DR   PANTHER; PTHR22599; PTHR22599; 1.
DR   Pfam; PF03637; Mob1_phocein; 1.
DR   SMART; SM01388; Mob1_phocein; 1.
DR   SUPFAM; SSF101152; SSF101152; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT   CHAIN           2..216
FT                   /note="MOB kinase activator 1A"
FT                   /id="PRO_0000247604"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT   MOD_RES         35
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT   MOD_RES         74
FT                   /note="Phosphothreonine; by STK3/MST2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT   MOD_RES         181
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
SQ   SEQUENCE   216 AA;  25080 MW;  58043AECAD1F5987 CRC64;
     MSFLFSSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRQAVMLPEG EDLNEWIAVN
     TVDFFNQINM LYGTITEFCT EASCPVMSAG PRYEYHWADG TNIKKPIKCS APKYIDYLMT
     WVQDQLDDET LFPSKIGVPF PKNFMSVAKT ILKRLFRVYA HIYHQHFDSV MQLQEEAHLN
     TSFKHFIFFV QEFNLIDRRE LAPLQELIEK LGSKDR