OPHN1_MOUSE
ID OPHN1_MOUSE Reviewed; 802 AA.
AC Q99J31; Q544K7;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Oligophrenin-1;
GN Name=Ophn1;
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=Cerebellum, Eye, and Testis;
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NR1D1.
RX PubMed=21874017; DOI=10.1038/nn.2911;
RA Valnegri P., Khelfaoui M., Dorseuil O., Bassani S., Lagneaux C.,
RA Gianfelice A., Benfante R., Chelly J., Billuart P., Sala C., Passafaro M.;
RT "A circadian clock in hippocampus is regulated by interaction between
RT oligophrenin-1 and Rev-erbalpha.";
RL Nat. Neurosci. 14:1293-1301(2011).
CC -!- FUNCTION: Stimulates GTP hydrolysis of members of the Rho family. Its
CC action on RHOA activity and signaling is implicated in growth and
CC stabilization of dendritic spines, and therefore in synaptic function.
CC Critical for the stabilization of AMPA receptors at postsynaptic sites.
CC Critical for the regulation of synaptic vesicle endocytosis at
CC presynaptic terminals (By similarity). Required for the localization of
CC NR1D1 to dendrites, can suppress its repressor activity and protect it
CC from proteasomal degradation. {ECO:0000250,
CC ECO:0000269|PubMed:21874017}.
CC -!- SUBUNIT: Interacts with HOMER1. Interacts with AMPA receptor complexes.
CC Interacts with SH3GL2 (endophilin-A1) (By similarity). Interacts (via
CC C-terminus) with NR1D1. {ECO:0000250, ECO:0000269|PubMed:21874017}.
CC -!- SUBCELLULAR LOCATION: Postsynapse {ECO:0000269|PubMed:21874017}.
CC Presynapse {ECO:0000269|PubMed:21874017}. Cell projection, axon
CC {ECO:0000269|PubMed:21874017}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:21874017}. Cell projection, dendrite
CC {ECO:0000269|PubMed:21874017}. Cytoplasm {ECO:0000269|PubMed:21874017}.
CC Note=Present in both presynaptic and postsynaptic sites. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK031419; BAC27395.1; -; mRNA.
DR EMBL; AK036038; BAC29282.1; -; mRNA.
DR EMBL; AK087469; BAC39887.1; -; mRNA.
DR EMBL; BC004845; AAH04845.1; -; mRNA.
DR CCDS; CCDS30295.1; -.
DR RefSeq; NP_001300683.1; NM_001313754.1.
DR RefSeq; NP_001300684.1; NM_001313755.1.
DR RefSeq; NP_001300685.1; NM_001313756.1.
DR RefSeq; NP_443208.1; NM_052976.4.
DR AlphaFoldDB; Q99J31; -.
DR SMR; Q99J31; -.
DR BioGRID; 220466; 34.
DR IntAct; Q99J31; 5.
DR MINT; Q99J31; -.
DR STRING; 10090.ENSMUSP00000033560; -.
DR iPTMnet; Q99J31; -.
DR PhosphoSitePlus; Q99J31; -.
DR MaxQB; Q99J31; -.
DR PaxDb; Q99J31; -.
DR PRIDE; Q99J31; -.
DR ProteomicsDB; 294277; -.
DR Antibodypedia; 494; 115 antibodies from 24 providers.
DR DNASU; 94190; -.
DR Ensembl; ENSMUST00000033560; ENSMUSP00000033560; ENSMUSG00000031214.
DR Ensembl; ENSMUST00000113826; ENSMUSP00000109457; ENSMUSG00000031214.
DR GeneID; 94190; -.
DR KEGG; mmu:94190; -.
DR UCSC; uc009tux.1; mouse.
DR CTD; 4983; -.
DR MGI; MGI:2151070; Ophn1.
DR VEuPathDB; HostDB:ENSMUSG00000031214; -.
DR eggNOG; KOG1451; Eukaryota.
DR GeneTree; ENSGT00940000160157; -.
DR HOGENOM; CLU_011532_2_1_1; -.
DR InParanoid; Q99J31; -.
DR OMA; MKRMKQP; -.
DR OrthoDB; 693048at2759; -.
DR PhylomeDB; Q99J31; -.
DR TreeFam; TF316851; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 94190; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ophn1; mouse.
DR PRO; PR:Q99J31; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q99J31; protein.
DR Bgee; ENSMUSG00000031214; Expressed in animal zygote and 240 other tissues.
DR ExpressionAtlas; Q99J31; baseline and differential.
DR Genevisible; Q99J31; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IMP:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; ISO:MGI.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; ISO:MGI.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; ISO:MGI.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0098880; P:maintenance of postsynaptic specialization structure; ISO:MGI.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:MGI.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:MGI.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Endocytosis; GTPase activation; Neurogenesis;
KW Reference proteome; Synapse.
FT CHAIN 1..802
FT /note="Oligophrenin-1"
FT /id="PRO_0000056761"
FT DOMAIN 265..368
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 380..564
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 606..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..755
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ 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
