PSD3_MOUSE
ID PSD3_MOUSE Reviewed; 1037 AA.
AC Q2PFD7; Q3TTA1; Q80TN6; Q80UZ7; Q8CEA6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=PH and SEC7 domain-containing protein 3;
DE AltName: Full=Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 D;
DE Short=Exchange factor for ARF6 D;
DE AltName: Full=Pleckstrin homology and SEC7 domain-containing protein 3;
GN Name=Psd3; Synonyms=Efa6d {ECO:0000303|PubMed:23603394}, Kiaa0942;
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 [MRNA] (ISOFORM 5), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16707115; DOI=10.1016/j.brainres.2006.02.058;
RA Sakagami H., Suzuki H., Kamata A., Owada Y., Fukunaga K., Mayanagi H.,
RA Kondo H.;
RT "Distinct spatiotemporal expression of EFA6D, a guanine nucleotide exchange
RT factor for ARF6, among the EFA6 family in mouse brain.";
RL Brain Res. 1093:1-11(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-729 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-1037 (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 823-1037 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759; SER-998; SER-1000;
RP SER-1001; SER-1003 AND SER-1009, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, 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).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=23603394; DOI=10.1016/j.febslet.2013.03.042;
RA Ueda T., Hanai A., Takei T., Kubo K., Ohgi M., Sakagami H., Takahashi S.,
RA Shin H.W., Nakayama K.;
RT "EFA6 activates Arf6 and participates in its targeting to the Flemming body
RT during cytokinesis.";
RL FEBS Lett. 587:1617-1623(2013).
CC -!- FUNCTION: Guanine nucleotide exchange factor for ARF6.
CC {ECO:0000269|PubMed:16707115}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23603394}. Cell
CC projection, ruffle membrane {ECO:0000269|PubMed:23603394}. Postsynaptic
CC density {ECO:0000269|PubMed:16707115}. Note=In interphase associated
CC with the plasma membrane, in particular with membrane ruffling regions.
CC {ECO:0000269|PubMed:23603394}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q2PFD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2PFD7-2; Sequence=VSP_029160;
CC Name=3;
CC IsoId=Q2PFD7-3; Sequence=VSP_029157, VSP_029159, VSP_029160;
CC Name=4;
CC IsoId=Q2PFD7-4; Sequence=VSP_029161;
CC Name=5;
CC IsoId=Q2PFD7-5; Sequence=VSP_029158;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC liver. Present in brain, with highest levels in olfactory bulb, cortex,
CC hippocampal pyramidal cell layer and cerebellar granule cell layer (at
CC protein level). {ECO:0000269|PubMed:16707115}.
CC -!- DEVELOPMENTAL STAGE: Expressed only in spinal cord at 13 dpc. At 18 dpc
CC and P0, appears weakly in forebrain. Expression in brain increases
CC after birth and peaks at P10. {ECO:0000269|PubMed:16707115}.
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DR EMBL; AB220685; BAE73186.1; -; mRNA.
DR EMBL; AK028684; BAC26065.1; -; mRNA.
DR EMBL; AK161498; BAE36424.1; -; mRNA.
DR EMBL; AK122405; BAC65687.1; -; mRNA.
DR EMBL; BC042208; AAH42208.1; -; mRNA.
DR CCDS; CCDS22340.1; -. [Q2PFD7-3]
DR CCDS; CCDS40355.3; -. [Q2PFD7-5]
DR RefSeq; NP_081902.1; NM_027626.1.
DR RefSeq; NP_084539.2; NM_030263.5. [Q2PFD7-3]
DR RefSeq; NP_808366.2; NM_177698.4. [Q2PFD7-5]
DR RefSeq; XP_017168191.1; XM_017312702.1. [Q2PFD7-2]
DR AlphaFoldDB; Q2PFD7; -.
DR SMR; Q2PFD7; -.
DR BioGRID; 231513; 3.
DR IntAct; Q2PFD7; 2.
DR MINT; Q2PFD7; -.
DR STRING; 10090.ENSMUSP00000091178; -.
DR iPTMnet; Q2PFD7; -.
DR PhosphoSitePlus; Q2PFD7; -.
DR SwissPalm; Q2PFD7; -.
DR jPOST; Q2PFD7; -.
DR MaxQB; Q2PFD7; -.
DR PaxDb; Q2PFD7; -.
DR PeptideAtlas; Q2PFD7; -.
DR PRIDE; Q2PFD7; -.
DR ProteomicsDB; 291692; -. [Q2PFD7-1]
DR ProteomicsDB; 291693; -. [Q2PFD7-2]
DR ProteomicsDB; 291694; -. [Q2PFD7-3]
DR ProteomicsDB; 291695; -. [Q2PFD7-4]
DR ProteomicsDB; 291696; -. [Q2PFD7-5]
DR Antibodypedia; 9043; 153 antibodies from 22 providers.
DR DNASU; 234353; -.
DR Ensembl; ENSMUST00000093468; ENSMUSP00000091178; ENSMUSG00000030465. [Q2PFD7-3]
DR Ensembl; ENSMUST00000093469; ENSMUSP00000091179; ENSMUSG00000030465. [Q2PFD7-5]
DR Ensembl; ENSMUST00000098696; ENSMUSP00000096293; ENSMUSG00000030465. [Q2PFD7-5]
DR GeneID; 234353; -.
DR KEGG; mmu:234353; -.
DR UCSC; uc009lvz.2; mouse. [Q2PFD7-3]
DR UCSC; uc009lwc.1; mouse. [Q2PFD7-2]
DR UCSC; uc057alt.1; mouse. [Q2PFD7-5]
DR CTD; 23362; -.
DR MGI; MGI:1918215; Psd3.
DR VEuPathDB; HostDB:ENSMUSG00000030465; -.
DR eggNOG; KOG0932; Eukaryota.
DR GeneTree; ENSGT00940000156591; -.
DR HOGENOM; CLU_011021_1_1_1; -.
DR InParanoid; Q2PFD7; -.
DR OMA; YDIYVSI; -.
DR PhylomeDB; Q2PFD7; -.
DR TreeFam; TF319755; -.
DR BioGRID-ORCS; 234353; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Psd3; mouse.
DR PRO; PR:Q2PFD7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q2PFD7; protein.
DR Bgee; ENSMUSG00000030465; Expressed in subiculum and 235 other tissues.
DR ExpressionAtlas; Q2PFD7; baseline and differential.
DR Genevisible; Q2PFD7; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0032011; P:ARF protein signal transduction; IC:MGI.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..1037
FT /note="PH and SEC7 domain-containing protein 3"
FT /id="PRO_0000309454"
FT DOMAIN 515..723
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 774..887
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 37..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 911..941
FT /evidence="ECO:0000255"
FT COMPBIAS 262..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYI0"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..518
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029157"
FT VAR_SEQ 1..44
FT /note="MEGRNAAAEPFVWVNSASAHSQSVAKAKYEFLFGKSEEKTPDSS -> MGNC
FT WSYSNLC (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16707115"
FT /id="VSP_029158"
FT VAR_SEQ 519..530
FT /note="TRGPQEIAFWGS -> MGIIMCLIYCYC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029159"
FT VAR_SEQ 684
FT /note="Missing (in isoform 3 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029160"
FT VAR_SEQ 919..966
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_029161"
FT CONFLICT 190
FT /note="D -> E (in Ref. 2; BAC26065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1037 AA; 114722 MW; E6E3C240AC7A61E8 CRC64;
MEGRNAAAEP FVWVNSASAH SQSVAKAKYE FLFGKSEEKT PDSSDHGGST LLPPTVTNEF
PEYGTMEEGG EGLRASLDFD AKSPPCRLPG QQAVHLLAGQ DSILNSVTEG PNDAPQCHPQ
EQSLQPIDSL ISALKATEAR IASGTFQATK VLDKDANFSV YQVDKELSTA SHKPQRAHRT
FPVGPGKSPD IPLSAEVPTE ENLSLHIQED LSALLPEEAQ AHRSQITNYR RQGPLRVPES
ACPVSSSSAG SHNPVDRVGA LREQRSDLGR EHPRGYDRGG SMGRQGRIKH VEFQGVEILW
TGEEAESRHP PERTASPVSK EFAKRPSHSS PACGVCSTST HLTGDVWDET CKAPSERPGT
SAGTLSPMPL GESGEDDVFL RESKEHLEEN FAIQGDKERI LDQEEHLRGD DDILGPGYTE
DSTDVYSSQF ETILDNTSLY YSAESLETLY SEPDSYFSFE MPLTPMIQQR IKEGGQFLER
TSVGGQHDVL SVSADGGIVM GYSAGITNGL HDSANSVYTR GPQEIAFWGS RDRCFAEGKT
TGVDAGSEMG STDILEKETT ESLSNGTNSN VEAAKRLAKR LYHLDRFKRS DVAKHLGKNN
EFSKLVAEEY LKFFDFTGMT LDQSLRYFLK AFSLVGETQE RERVLIHFSN RYFSCNPDTI
TSKDGVHCLT CAMMLLNTDL HGHVNIGKKM TCQEFITNLQ GVNEGGDFSK DLLKALYNSI
KNEKLEWAVD DEEKKKSPSE GTDEKANGTH PKTISRIGST TNPFLDIPHD PNAAVYKSGF
LARKIHADMD GKKTPRGKRG WKTFYAVLKG TVLYLQKDEY KPEKSLSDED LKNAVSVHHA
LASKATDYEK KPNVFKLKTA DWRVLLFQTQ SPEEMQGWIN KINCVAAVFS APPFPAAIGS
QKKFSRPLLP ATTTKLSQEE QLKSHESKLK QITTELAEHR SYPPDKKVKA KDVDEYKLKD
HYLEFEKTRY EIYVSVLKEG GKELLTTDGN EPVGLKKSHS SPSLNPDASP VTAKVKRNVS
ERKDHRPETP GIKQKVT
