PHOCN_RAT
ID PHOCN_RAT Reviewed; 225 AA.
AC Q9QYW3;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=MOB-like protein phocein;
DE AltName: Full=Class II mMOB1;
DE AltName: Full=Mob1 homolog 3;
DE Short=Mob3;
DE AltName: Full=Mps one binder kinase activator-like 3;
DE AltName: Full=Phocein;
DE AltName: Full=Preimplantation protein 3;
GN Name=Mob4; Synonyms=Mob3, Mobkl1, Phocn, Prei3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STRN; STRN3 AND STRN4, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=11251078; DOI=10.1091/mbc.12.3.663;
RA Baillat G., Moqrich A., Castets F., Baude A., Bailly Y., Benmerah A.,
RA Monneron A.;
RT "Molecular cloning and characterization of phocein, a protein found from
RT the Golgi complex to dendritic spines.";
RL Mol. Biol. Cell 12:663-673(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INTERACTION WITH DNM1 AND EPS15, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11872741; DOI=10.1074/jbc.m108818200;
RA Baillat G., Gaillard S., Castets F., Monneron A.;
RT "Interactions of phocein with nucleoside-diphosphate kinase, Eps15, and
RT Dynamin I.";
RL J. Biol. Chem. 277:18961-18966(2002).
RN [4]
RP INTERACTION WITH CTTNBP2.
RX PubMed=23015759; DOI=10.1091/mbc.e12-05-0365;
RA Chen Y.K., Chen C.Y., Hu H.T., Hsueh Y.P.;
RT "CTTNBP2, but not CTTNBP2NL, regulates dendritic spinogenesis and synaptic
RT distribution of the striatin-PP2A complex.";
RL Mol. Biol. Cell 23:4383-4392(2012).
CC -!- FUNCTION: May play a role in membrane trafficking, specifically in
CC membrane budding reactions. {ECO:0000269|PubMed:11872741}.
CC -!- SUBUNIT: Binds STRN, STRN3 and STRN4. Part of a ternary complex
CC containing MOB4/PHOCN, STRN and/or STRN3 and PPA2. Interacts with DNM1
CC and EPS15. Interacts with nucleoside diphosphate kinase. Interacts with
CC CTTNBP2. Interacts with CTTNBP2NL (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Golgi apparatus, Golgi stack membrane; Peripheral membrane protein.
CC Note=Detected in cell bodies and dendrites of neurons, but not in
CC axons.
CC -!- TISSUE SPECIFICITY: Highly expressed in adrenal gland, spinal cord,
CC brain and cerebellum. Detected at lower levels in heart and skeletal
CC muscle, and at very low levels in spleen, liver and intestine.
CC {ECO:0000269|PubMed:11251078}.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR EMBL; AJ132008; CAB57295.1; -; mRNA.
DR EMBL; BC085708; AAH85708.1; -; mRNA.
DR RefSeq; NP_598212.1; NM_133528.1.
DR AlphaFoldDB; Q9QYW3; -.
DR SMR; Q9QYW3; -.
DR BioGRID; 251067; 4.
DR MINT; Q9QYW3; -.
DR STRING; 10116.ENSRNOP00000020536; -.
DR iPTMnet; Q9QYW3; -.
DR PhosphoSitePlus; Q9QYW3; -.
DR SwissPalm; Q9QYW3; -.
DR jPOST; Q9QYW3; -.
DR PaxDb; Q9QYW3; -.
DR PRIDE; Q9QYW3; -.
DR Ensembl; ENSRNOT00000103898; ENSRNOP00000092795; ENSRNOG00000014980.
DR GeneID; 171050; -.
DR KEGG; rno:171050; -.
DR UCSC; RGD:620183; rat.
DR CTD; 25843; -.
DR RGD; 620183; Mob4.
DR eggNOG; KOG1852; Eukaryota.
DR GeneTree; ENSGT01050000244956; -.
DR HOGENOM; CLU_056981_3_0_1; -.
DR InParanoid; Q9QYW3; -.
DR OMA; CKRFTTY; -.
DR OrthoDB; 1229701at2759; -.
DR PhylomeDB; Q9QYW3; -.
DR TreeFam; TF314078; -.
DR PRO; PR:Q9QYW3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000014980; Expressed in ovary and 20 other tissues.
DR Genevisible; Q9QYW3; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006900; P:vesicle budding from membrane; TAS:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Transport; Zinc.
FT CHAIN 1..225
FT /note="MOB-like protein phocein"
FT /id="PRO_0000193578"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 225 AA; 26032 MW; D0EF1219711458BA CRC64;
MVMAEGTAVL RRNRPGTKAQ DFYNWPDESF DEMDSTLAVQ QYIQQNIRAD CSNIDKILEP
PEGQDEGVWK YEHLRQFCLE LNGLAVKLQS ECHPDTCTQM TATEQWIFLC AAHKTPKECP
AIDYTRHTLD GAACLLNSNK YFPSRVSIKE SSVAKLGSVC RRIYRIFSHA YFHHRQIFDE
YENETFLCHR FTKFVMKYNL MSKDNLIVPI LEEEVQNSVS GESEA
