PHOCN_MOUSE
ID PHOCN_MOUSE Reviewed; 225 AA.
AC Q6PEB6; Q3TS21; Q8BSA3; Q9CX28;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=Preimplantation protein 3;
GN Name=Mob4; Synonyms=Mob3, Mobkl3, Phocn, Prei3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland, and Mammary tumor;
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 INTERACTION WITH STRN; STRN3 AND THE PPA2 COMPLEX, PHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11319234; DOI=10.1074/jbc.m102398200;
RA Moreno C.S., Lane W.S., Pallas D.C.;
RT "A mammalian homolog of yeast MOB1 is both a member and a putative
RT substrate of striatin family-protein phosphatase 2A complexes.";
RL J. Biol. Chem. 276:24253-24260(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in membrane trafficking, specifically in
CC membrane budding reactions.
CC -!- SUBUNIT: Binds STRN4 (By similarity). Interacts with DNM1 and EPS15 (By
CC similarity). Interacts with nucleoside diphosphate kinase (By
CC similarity). Binds STRN and STRN3. Part of a ternary complex containing
CC MOB4/PHOCN, STRN and/or STRN3 and PPA2. Interacts with CTTNBP2 and
CC CTTNBP2NL (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11319234}. Membrane {ECO:0000269|PubMed:11319234};
CC Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Golgi
CC apparatus, Golgi stack membrane {ECO:0000269|PubMed:11319234};
CC Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Note=In a
CC perinuclear punctate pattern. Associated with membranes and the Golgi
CC stacks.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:11319234}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR EMBL; AK020446; BAB32105.1; -; mRNA.
DR EMBL; AK034840; BAC28849.1; -; mRNA.
DR EMBL; AK162327; BAE36855.1; -; mRNA.
DR EMBL; BC037499; AAH37499.1; -; mRNA.
DR EMBL; BC058168; AAH58168.1; -; mRNA.
DR CCDS; CCDS14960.1; -.
DR RefSeq; NP_079559.2; NM_025283.3.
DR AlphaFoldDB; Q6PEB6; -.
DR SMR; Q6PEB6; -.
DR BioGRID; 202356; 5.
DR IntAct; Q6PEB6; 2.
DR STRING; 10090.ENSMUSP00000125415; -.
DR iPTMnet; Q6PEB6; -.
DR PhosphoSitePlus; Q6PEB6; -.
DR EPD; Q6PEB6; -.
DR MaxQB; Q6PEB6; -.
DR PaxDb; Q6PEB6; -.
DR PRIDE; Q6PEB6; -.
DR ProteomicsDB; 288145; -.
DR DNASU; 19070; -.
DR Ensembl; ENSMUST00000162364; ENSMUSP00000125415; ENSMUSG00000025979.
DR GeneID; 19070; -.
DR KEGG; mmu:19070; -.
DR UCSC; uc007bad.1; mouse.
DR CTD; 25843; -.
DR MGI; MGI:104899; Mob4.
DR VEuPathDB; HostDB:ENSMUSG00000025979; -.
DR eggNOG; KOG1852; Eukaryota.
DR GeneTree; ENSGT01050000244956; -.
DR InParanoid; Q6PEB6; -.
DR OMA; CKRFTTY; -.
DR OrthoDB; 1229701at2759; -.
DR PhylomeDB; Q6PEB6; -.
DR TreeFam; TF314078; -.
DR BioGRID-ORCS; 19070; 20 hits in 70 CRISPR screens.
DR ChiTaRS; Mob4; mouse.
DR PRO; PR:Q6PEB6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6PEB6; protein.
DR Bgee; ENSMUSG00000025979; Expressed in dorsal pancreas and 248 other tissues.
DR ExpressionAtlas; Q6PEB6; baseline and differential.
DR Genevisible; Q6PEB6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_0000193577"
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"
FT CONFLICT 142
FT /note="F -> S (in Ref. 1; BAB32105)"
FT /evidence="ECO:0000305"
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
