ID   OPHN1_PONPY             Reviewed;         802 AA.
AC   Q7YQL5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Oligophrenin-1;
GN   Name=OPHN1;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12777533; DOI=10.1093/molbev/msg134;
RA   Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT   "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT   chimpanzees.";
RL   Mol. Biol. Evol. 20:1281-1289(2003).
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 pre-
CC       synaptic terminals. Required for the localization of NR1D1 to
CC       dendrites, can suppress its repressor activity and protect it from
CC       proteasomal degradation (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynapse {ECO:0000250|UniProtKB:P0CAX5}.
CC       Presynapse {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, dendritic spine
CC       {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q99J31}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q99J31}.
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; AB102658; BAC81127.1; -; mRNA.
DR   AlphaFoldDB; Q7YQL5; -.
DR   SMR; Q7YQL5; -.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell projection; Cytoplasm; Endocytosis; GTPase activation; Neurogenesis;
KW   Synapse.
FT   CHAIN           1..802
FT                   /note="Oligophrenin-1"
FT                   /id="PRO_0000056763"
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          569..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..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        734..755
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   802 AA;  91615 MW;  05D03C6C98070064 CRC64;
     MGHPPLEFSD CYLDSPDFRE RLKCYEQELE RTNKFIKDVI KDGNALISAM RNYSSAVQKF
     SQTLQSFQFD FIGDTLTDDE INIAESFKEF AELLNEVENE RMMMVHNASD LLIKPLENFR
     KEQIGFTKER KKKFEKDGER FYSLLDRHLH LSSKKKESQL QEADLQVDKE RHNFFESSLD
     YVYQIQEVQE SKKFNIVEPV LAFLHSLFIS NSLTVELTQD FLPYKQQLQL SLQNTRNHFS
     STREEMEELK KRMKEAPQTC KLPGQPTIEG YLYTQEKWAL GISWVKYYCQ YEKETKTLTM
     TPMEQKPGAK QGPLDLTLKY CVRRKTESID KRFCFDIETN ERPGTITLQA LSEANRRLWM
     EAMDGKEPIY HSPITKQQEM ELNEVGFKFV RKCINIIETK GIKTEGLYRT VGSNIQVQKL
     LNAFFDPKCP GDVDFHNSDW DIKTITSSLK FYLRNLSEPV MTYRLHKELV SAAKSDNLDY
     RLGAIHSLVY KLPEKNREML ELLIRHLVNV CEHSKENLMT PSNMGVIFGP TLMRAQEDTV
     AAMMNIKFQN IVVEILIEHF GKIYLGPPEE SAAPPVPPPR VTARRHKPIT ISKRLLRERT
     VFYTSSLDES EDEIQHQTPN GTITSSIEPP KPPQHPKLPI QRSGETDPGR KSPSRPISDG
     KLEPCPEVDV GKLVSRLQDG GTKITPKATN GPMPGSGPTK TPSFHIKRPA PRPLAHHKEG
     DADSFSKVRP PGEKPTIIRP PVRPPDPPCR AATPQKPEPK PDIVAGNAGE ITSSVVASRT
     RFFETASRKT GSSQGRLPGD ES