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Database: UniProt
Entry: Q14CM0
LinkDB: Q14CM0
Original site: Q14CM0 
ID   FRPD4_HUMAN             Reviewed;        1322 AA.
AC   Q14CM0; A8K0X9; O15032;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   01-OCT-2014, entry version 73.
DE   RecName: Full=FERM and PDZ domain-containing protein 4;
DE   AltName: Full=PDZ domain-containing protein 10;
DE   AltName: Full=PSD-95-interacting regulator of spine morphogenesis;
DE            Short=Preso;
GN   Name=FRMPD4; Synonyms=KIAA0316, PDZD10, PDZK10;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R., Nomura N.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Amygdala;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, INTERACTION WITH DLG1; DLG2; DLG3; DLG4; ARHGEF7 AND
RP   PHOSPHATIDYLINOSITOL-4,5-BIPHOSPHATE, DOMAIN FERM, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF ARG-102; 1319-GLU--VAL-1322 AND THR-1320.
RX   PubMed=19118189; DOI=10.1523/JNEUROSCI.3112-08.2008;
RA   Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y.,
RA   Kang G.B., Eom S.H., Kim H., Kim E.;
RT   "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT   regulates dendritic spine morphogenesis.";
RL   J. Neurosci. 28:14546-14556(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
CC   -!- FUNCTION: Positive regulator of dendritic spine morphogenesis and
CC       density. Required for the maintenance of excitatory synaptic
CC       transmission. Binds phosphatidylinositol 4,5-bisphosphate.
CC       {ECO:0000269|PubMed:19118189}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with DLG1, DLG2, DLG3 and
CC       DLG4/PSD95. Interacts (via N-terminus) with ARHGEF7; the
CC       interaction is mediated by the PDZ domain.
CC       {ECO:0000269|PubMed:19118189}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC       {ECO:0000269|PubMed:19118189}.
CC   -!- DOMAIN: The FERM domain mediates the interaction with
CC       phosphatidylinositol 4,5-bisphosphate.
CC       {ECO:0000269|PubMed:19118189}.
CC   -!- SIMILARITY: Contains 1 FERM domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00084}.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00143}.
CC   -!- SIMILARITY: Contains 1 WW domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00224}.
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DR   EMBL; AB002314; BAA20774.3; -; mRNA.
DR   EMBL; AK289694; BAF82383.1; -; mRNA.
DR   EMBL; BC113700; AAI13701.1; -; mRNA.
DR   EMBL; BC113702; AAI13703.1; -; mRNA.
DR   CCDS; CCDS35201.1; -.
DR   RefSeq; NP_055543.2; NM_014728.3.
DR   UniGene; Hs.657507; -.
DR   ProteinModelPortal; Q14CM0; -.
DR   SMR; Q14CM0; 33-66, 87-151, 206-442.
DR   BioGrid; 115105; 2.
DR   IntAct; Q14CM0; 4.
DR   MINT; MINT-2795491; -.
DR   STRING; 9606.ENSP00000370057; -.
DR   PhosphoSite; Q14CM0; -.
DR   DMDM; 121948742; -.
DR   MaxQB; Q14CM0; -.
DR   PaxDb; Q14CM0; -.
DR   PRIDE; Q14CM0; -.
DR   DNASU; 9758; -.
DR   Ensembl; ENST00000380682; ENSP00000370057; ENSG00000169933.
DR   GeneID; 9758; -.
DR   KEGG; hsa:9758; -.
DR   UCSC; uc004cuz.2; human.
DR   CTD; 9758; -.
DR   GeneCards; GC0XP012066; -.
DR   H-InvDB; HIX0016653; -.
DR   HGNC; HGNC:29007; FRMPD4.
DR   HPA; HPA035580; -.
DR   MIM; 300838; gene.
DR   neXtProt; NX_Q14CM0; -.
DR   PharmGKB; PA134977575; -.
DR   eggNOG; NOG237011; -.
DR   HOGENOM; HOG000090222; -.
DR   HOVERGEN; HBG106593; -.
DR   OMA; QETGTEN; -.
DR   OrthoDB; EOG7W419W; -.
DR   PhylomeDB; Q14CM0; -.
DR   TreeFam; TF316497; -.
DR   ChiTaRS; FRMPD4; human.
DR   GenomeRNAi; 9758; -.
DR   NextBio; 36727; -.
DR   PRO; PR:Q14CM0; -.
DR   Bgee; Q14CM0; -.
DR   CleanEx; HS_FRMPD4; -.
DR   Genevestigator; Q14CM0; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0051835; P:positive regulation of synapse structural plasticity; IMP:UniProtKB.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   InterPro; IPR001202; WW_dom.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Complete proteome; Lipid-binding; Reference proteome.
FT   CHAIN         1   1322       FERM and PDZ domain-containing protein 4.
FT                                /FTId=PRO_0000307132.
FT   DOMAIN       33     66       WW. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   DOMAIN       78    155       PDZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      204    519       FERM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00084}.
FT   MUTAGEN     102    102       R->A: Abolishes the interaction with
FT                                ARHGEF7. Mutant overexpression in
FT                                cultured neurons does not induce a
FT                                significant increase in spine density
FT                                contrary to wild type.
FT                                {ECO:0000269|PubMed:19118189}.
FT   MUTAGEN    1319   1322       Missing: Abolishes the interaction with
FT                                DLG1, DLG2, DLG3 and DLG4/PSD95. Reduces
FT                                protein localization to dendritic spines.
FT   MUTAGEN    1320   1320       T->D: Abolishes the interaction with
FT                                DLG4/PSD95. Reduces protein localization
FT                                to dendritic spines.
FT                                {ECO:0000269|PubMed:19118189}.
FT   CONFLICT    130    130       A -> T (in Ref. 1; BAA20774).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1322 AA;  144379 MW;  79B73E41B89E2D08 CRC64;
     MDVFSFVKIA KLSSHRTKSS GWPPPSGTWG LSQVPPYGWE MTANRDGRDY FINHMTQAIP
     FDDPRLESCQ IIPPAPRKVE MRRDPVLGFG FVAGSEKPVV VRSVTPGGPS EGKLIPGDQI
     VMINDEPVSA APRERVIDLV RSCKESILLT VIQPYPSPKS AFISAAKKAR LKSNPVKVRF
     SEEVIINGQV SETVKDNSLL FMPNVLKVYL ENGQTKSFRF DCSTSIKDVI LTLQEKLSIK
     GIEHFSLMLE QRTEGAGTKL LLLHEQETLT QVTQRPSSHK MRCLFRISFV PKDPIDLLRR
     DPVAFEYLYV QSCNDVVQER FGPELKYDIA LRLAALQMYI ATVTTKQTQK ISLKYIEKEW
     GLETFLPSAV LQSMKEKNIK KALSHLVKAN QNLVPPGKKL SALQAKVHYL KFLSDLRLYG
     GRVFKATLVQ AEKRSEVTLL VGPRYGISHV INTKTNLVAL LADFSHVNRI EMFSEEESLV
     RVELHVLDVK PITLLMESSD AMNLACLTAG YYRLLVDSRR SIFNMANKKN TATQETGPEN
     KGKHNLLGPD WNCIPQMTTF IGEGEQEAQI TYIDSKQKTV EITDSTMCPK EHRHLYIDNA
     YSSDGLNQQL SQPGEAPCEA DYRSLAQRSL LTLSGPETLK KAQESPRGAK VSFIFGDFAL
     DDGISPPTLG YETLLDEGPE MLEKQRNLYI GSANDMKGLD LTPEAEGIQF VENSVYANIG
     DVKSFQAAEG IEEPLLHDIC YAENTDDAED EDEVSCEEDL VVGEMNQPAI LNLSGSSDDI
     IDLTSLPPPE GDDNEDDFLL RSLNMAIAAP PPGFRDSSDE EDSQSQAASF PEDKEKGSSL
     QNDEIPVSLI DAVPTSAEGK CEKGLDNAVV STLGALEALS VSEEQQTSDN SGVAILRAYS
     PESSSDSGNE TNSSEMTESS ELATAQKQSE NLSRMFLATH EGYHPLAEEQ TEFPASKTPA
     GGLPPKSSHA LAARPATDLP PKVVPSKQLL HSDHMEMEPE TMETKSVTDY FSKLHMGSVA
     YSCTSKRKSK LADGEGKAPP NGNTTGKKQQ GTKTAEMEEE ASGKFGTVSS RDSQHLSTFN
     LERTAFRKDS QRWYVATEGG MAEKSGLEAA TGKTFPRASG LGAREAEGKE EGAPDGETSD
     GSGLGQGDRF LTDVTCASSA KDLDNPEDAD SSTCDHPSKL PEADESVARL CDYHLAKRMS
     SLQSEGHFSL QSSQGSSVDA GCGTGSSGSA CATPVESPLC PSLGKHLIPD ASGKGVNYIP
     SEERAPGLPN HGATFKELHP QTEGMCPRMT VPALHTAINT EPLFGTLRDG CHRLPKIKET
     TV
//
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