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Oligophrenin-1

 OPHN1_MOUSE             Reviewed;         802 AA.
Q99J31; Q544K7;
11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
20-JUN-2018, entry version 136.
RecName: Full=Oligophrenin-1;
Name=Ophn1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum, Eye, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NR1D1.
PubMed=21874017; DOI=10.1038/nn.2911;
Valnegri P., Khelfaoui M., Dorseuil O., Bassani S., Lagneaux C.,
Gianfelice A., Benfante R., Chelly J., Billuart P., Sala C.,
Passafaro M.;
"A circadian clock in hippocampus is regulated by interaction between
oligophrenin-1 and Rev-erbalpha.";
Nat. Neurosci. 14:1293-1301(2011).
-!- FUNCTION: Stimulates GTP hydrolysis of members of the Rho family.
Its action on RHOA activity and signaling is implicated in growth
and stabilization of dendritic spines, and therefore in synaptic
function. Critical for the stabilization of AMPA receptors at
postsynaptic sites. Critical for the regulation of synaptic
vesicle endocytosis at presynaptic terminals (By similarity).
Required for the localization of NR1D1 to dendrites, can suppress
its repressor activity and protect it from proteasomal
degradation. {ECO:0000250, ECO:0000269|PubMed:21874017}.
-!- SUBUNIT: Interacts with HOMER1. Interacts with AMPA receptor
complexes. Interacts with SH3GL2 (endophilin-A1) (By similarity).
Interacts (via C-terminus) with NR1D1. {ECO:0000250,
ECO:0000269|PubMed:21874017}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse
{ECO:0000269|PubMed:21874017}. Cell projection, axon
{ECO:0000269|PubMed:21874017}. Cell projection, dendritic spine
{ECO:0000269|PubMed:21874017}. Cell projection, dendrite
{ECO:0000269|PubMed:21874017}. Cytoplasm
{ECO:0000269|PubMed:21874017}. Note=Present in both presynaptic
and postsynaptic sites. {ECO:0000250}.
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EMBL; AK031419; BAC27395.1; -; mRNA.
EMBL; AK036038; BAC29282.1; -; mRNA.
EMBL; AK087469; BAC39887.1; -; mRNA.
EMBL; BC004845; AAH04845.1; -; mRNA.
CCDS; CCDS30295.1; -.
RefSeq; NP_001300683.1; NM_001313754.1.
RefSeq; NP_001300684.1; NM_001313755.1.
RefSeq; NP_001300685.1; NM_001313756.1.
RefSeq; NP_443208.1; NM_052976.4.
UniGene; Mm.254336; -.
UniGene; Mm.33536; -.
ProteinModelPortal; Q99J31; -.
SMR; Q99J31; -.
BioGrid; 220466; 1.
IntAct; Q99J31; 1.
STRING; 10090.ENSMUSP00000033560; -.
iPTMnet; Q99J31; -.
PhosphoSitePlus; Q99J31; -.
MaxQB; Q99J31; -.
PaxDb; Q99J31; -.
PRIDE; Q99J31; -.
Ensembl; ENSMUST00000033560; ENSMUSP00000033560; ENSMUSG00000031214.
Ensembl; ENSMUST00000113826; ENSMUSP00000109457; ENSMUSG00000031214.
GeneID; 94190; -.
KEGG; mmu:94190; -.
UCSC; uc009tux.1; mouse.
CTD; 4983; -.
MGI; MGI:2151070; Ophn1.
eggNOG; KOG1451; Eukaryota.
eggNOG; ENOG410YJPS; LUCA.
GeneTree; ENSGT00920000148941; -.
HOGENOM; HOG000018767; -.
HOVERGEN; HBG067993; -.
InParanoid; Q99J31; -.
KO; K20650; -.
OMA; VRKCINA; -.
OrthoDB; EOG091G01TT; -.
PhylomeDB; Q99J31; -.
TreeFam; TF316851; -.
Reactome; R-MMU-194840; Rho GTPase cycle.
PRO; PR:Q99J31; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031214; -.
CleanEx; MM_OPHN1; -.
ExpressionAtlas; Q99J31; baseline and differential.
Genevisible; Q99J31; MM.
GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
GO; GO:0043195; C:terminal bouton; IDA:MGI.
GO; GO:0003779; F:actin binding; IDA:MGI.
GO; GO:0005096; F:GTPase activator activity; IMP:MGI.
GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
GO; GO:0005543; F:phospholipid binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; ISO:MGI.
GO; GO:0021707; P:cerebellar granule cell differentiation; ISO:MGI.
GO; GO:0021895; P:cerebral cortex neuron differentiation; ISO:MGI.
GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IDA:UniProtKB.
GO; GO:0030182; P:neuron differentiation; ISO:MGI.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:0030100; P:regulation of endocytosis; IMP:MGI.
GO; GO:0035023; P:regulation of Rho protein signal transduction; ISO:MGI.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:MGI.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:MGI.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
Pfam; PF00169; PH; 1.
Pfam; PF00620; RhoGAP; 1.
SMART; SM00233; PH; 1.
SMART; SM00324; RhoGAP; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50238; RHOGAP; 1.
1: Evidence at protein level;
Cell junction; Cell projection; Complete proteome; Cytoplasm;
Endocytosis; GTPase activation; Neurogenesis; Reference proteome;
Synapse.
CHAIN 1 802 Oligophrenin-1.
/FTId=PRO_0000056761.
DOMAIN 265 368 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 380 564 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
COMPBIAS 629 761 Pro-rich.
SEQUENCE 802 AA; 91985 MW; 08ECD6694F19B69C CRC64;
MGHPPLEFSD CYLDSPDFRQ RLKYYEEELE RTNKFIKDVI KDGSALISAM RNYSSAVQKF
SQTLQSFQFD FIGDTLTDDE INIAESFKEF AELLNEVENE RMMMVQNASD LLIKPLETFR
KEQIGFTKER KKKFEKDGER FYSLLDRHLH LSSKKKESQL LEADLQVDKE RHNFFESSLD
YVYQIQEVQE SKKFNIVEPV LAFLHSLFIS NSLTVELTQD FLPYKQQLQL SLQNTRNHFS
STREEMEELK KRMKEAPQTC KLPGQPTIEG YLYTQEKWAL GISWAKYYCR YEKETRMLTM
IPMEQKPGAK QGPVDLTLKY CVRRKTESID KRFCFDIETN ERPGTITLQA PSEANRRLWM
EAMDGKEPIY HTPITKQEEM ELNEVGFKFV RKCINFIETK GIKTEGLYRT VGSNIQVQKL
LYAFFDPKCP GDVDFHNSDW DIKTITSSLK FYLRNLSEPV MTYKLHKELV SAAKSDNLDY
RLGAIHSLVY KLPEKNREML ELLIKHLVNV CEHSKENLMT PSNMGVIFGP TLMRAQEDTV
AAMMNIKFQN IVVEILIEHF GKIYLGPPED SQVPPVPPPR VTARRHKPIT ISKRLLREKT
VFYTSSLDEN KDESHHQTPN GTITSNLDPP KLLQHLKPPM QKSGETDPGR KSPSRPVSDC
QSEPCLETDV GRLLFRLQDG GTKATPKASN GPVPGSGHTK TSSFHIRRPA PRPMAHHKEG
DTDGFSKVRP PGEKQTIIRP PVRPPDPPCR SITPQKPEPK PETGSGNADE IPSSVVASRT
RFFETASRKT GSSQGKLPGD ES


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