PSD4_MOUSE
ID PSD4_MOUSE Reviewed; 1005 AA.
AC Q8BLR5; A2AIU4; Q3TE33; Q3TQF5; Q3UD59; Q3UFH9; Q80V44;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=PH and SEC7 domain-containing protein 4;
DE AltName: Full=Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 B;
DE Short=Exchange factor for ARF6 B;
DE AltName: Full=Pleckstrin homology and SEC7 domain-containing protein 4;
GN Name=Psd4; Synonyms=Efa6b;
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, and NOD;
RC TISSUE=Bone marrow, Brain cortex, Pancreas, and Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-971, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
CC -!- FUNCTION: Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7.
CC Through ARL14 activation, controls the movement of MHC class II-
CC containing vesicles along the actin cytoskeleton in dendritic cells.
CC Involved in membrane recycling. Interacts with several
CC phosphatidylinositol phosphate species, including phosphatidylinositol
CC 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and
CC phosphatidylinositol 4,5-bisphosphate (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NDX1}.
CC Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8NDX1}.
CC Note=In interphase associated with the plasma membrane, in particular
CC with membrane ruffling regions. Accumulates in dynamic actin-rich
CC membrane ruffles and microvilli-like structures. Recruited to membranes
CC via phosphatidylinositol phosphate-binding.
CC {ECO:0000250|UniProtKB:Q8NDX1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE29402.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK043669; BAC31612.1; -; mRNA.
DR EMBL; AK148489; BAE28582.1; -; mRNA.
DR EMBL; AK150238; BAE29402.1; ALT_INIT; mRNA.
DR EMBL; AK163628; BAE37428.1; -; mRNA.
DR EMBL; AK169859; BAE41415.1; -; mRNA.
DR EMBL; AL732528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046518; AAH46518.1; -; mRNA.
DR EMBL; BC068231; AAH68231.1; -; mRNA.
DR CCDS; CCDS15737.1; -.
DR RefSeq; NP_808279.1; NM_177611.3.
DR RefSeq; XP_006497894.1; XM_006497831.3.
DR RefSeq; XP_006497895.1; XM_006497832.3.
DR RefSeq; XP_006497896.1; XM_006497833.3.
DR RefSeq; XP_006497897.1; XM_006497834.3.
DR RefSeq; XP_006497898.1; XM_006497835.3.
DR RefSeq; XP_006497899.1; XM_006497836.3.
DR RefSeq; XP_011237351.1; XM_011239049.2.
DR RefSeq; XP_017172556.1; XM_017317067.1.
DR AlphaFoldDB; Q8BLR5; -.
DR SMR; Q8BLR5; -.
DR BioGRID; 229642; 1.
DR IntAct; Q8BLR5; 1.
DR STRING; 10090.ENSMUSP00000062415; -.
DR iPTMnet; Q8BLR5; -.
DR PhosphoSitePlus; Q8BLR5; -.
DR EPD; Q8BLR5; -.
DR jPOST; Q8BLR5; -.
DR MaxQB; Q8BLR5; -.
DR PaxDb; Q8BLR5; -.
DR PeptideAtlas; Q8BLR5; -.
DR PRIDE; Q8BLR5; -.
DR ProteomicsDB; 291539; -.
DR Antibodypedia; 47549; 67 antibodies from 18 providers.
DR DNASU; 215632; -.
DR Ensembl; ENSMUST00000056641; ENSMUSP00000062415; ENSMUSG00000026979.
DR Ensembl; ENSMUST00000102942; ENSMUSP00000100006; ENSMUSG00000026979.
DR Ensembl; ENSMUST00000166388; ENSMUSP00000132395; ENSMUSG00000026979.
DR GeneID; 215632; -.
DR KEGG; mmu:215632; -.
DR UCSC; uc008ioy.1; mouse.
DR CTD; 23550; -.
DR MGI; MGI:2674093; Psd4.
DR VEuPathDB; HostDB:ENSMUSG00000026979; -.
DR eggNOG; KOG0932; Eukaryota.
DR GeneTree; ENSGT00940000161976; -.
DR HOGENOM; CLU_011021_2_0_1; -.
DR InParanoid; Q8BLR5; -.
DR OMA; SAQGEHR; -.
DR OrthoDB; 301851at2759; -.
DR PhylomeDB; Q8BLR5; -.
DR TreeFam; TF319755; -.
DR BioGRID-ORCS; 215632; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q8BLR5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BLR5; protein.
DR Bgee; ENSMUSG00000026979; Expressed in granulocyte and 108 other tissues.
DR ExpressionAtlas; Q8BLR5; baseline and differential.
DR Genevisible; Q8BLR5; MM.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 Cell membrane; Cell projection; Coiled coil;
KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1005
FT /note="PH and SEC7 domain-containing protein 4"
FT /id="PRO_0000251732"
FT DOMAIN 493..686
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 726..841
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 27..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 870..926
FT /evidence="ECO:0000255"
FT COMPBIAS 307..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX1"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX1"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX1"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX1"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX1"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 200
FT /note="F -> L (in Ref. 1; BAE41415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1005 AA; 112733 MW; 8D03C8C52917EB04 CRC64;
MMGDHLRPME CLNICLEDNL QPCPEAYPSE IHGHPGPSEP CQEHTCPFDP PESARPDAPH
GNSGVESTHL ENCLVQVQAR QASASLRSLE DNSSLGSPQQ NQSSSTQVVF WAGILQAQMC
VLDLEEELEK TEGLRAELRC CIPPPSKDLL GDEGLSPSRP EEDEDSGDDS SGPEEENQTW
PREKIPGSSL EWGAEEDSIF FDNPLFLESP CSDTSTEGEC FSWGYPNSHP DMKTWHQSPQ
TLDSPLQKGT GLWRQENELD LGSDTADHGG CSTPPFPVPS YKMHPCLALG STEGDPTVPP
DQEGETSCED DLGHGSPKAP FVDHELIQES DNFEFDLRPA TTHPVQPWGS QTSQSLSDLT
QPILEDLQRE DPSRSQETLI SQNRGERDAG CFQEPVFCTL APWGSQTSLL EPNCPESEGR
GSGPQPSPVS SQDSSPRVLL HSPKWPQDAS HLLQKDRSEL SSLKEEETEE VPSLRQEAEC
EDTSRSEDAS ANQHHVHLAS AEGLPESPMP QAQSPEEGWR PSSSREKLAN DIRNDKGAWN
LALRLYQLNG FRKSEVAAHL RKNNDFSRAV AEAYLSFFQF EGQSLDRALR GFLQALVLSG
ETQERERILY QFSKRFHYCN PGAFPSVDSV HTLTCAIMLL NTDLHGQNIG KSMSCQEFVT
NLNGLQDGRN FPKELLKALY WSIRSEKLEW AIDEEDADRP EKDQPSPSAG KISSPFLQMA
QDPTMPTYKQ GILARKMHHI ADGKKTPWGK RGWKMFHTLL RGMVLYFLKG EGQWLDGESL
VGHMVDEPVG VHHSLASPAT HYTKKPHVFQ LRTADWRLYL FQAPTAKEMA SWIARINLAA
ATHSAPPFPA AVGSQRRFVR PILPMSPVQS SLEEQHRSHE NCLDAASDDL LDLQRNLPER
RGRSRELEEY RLRKEYLEHE KTRYETYVQL LVARLHFPLG DLALWEDQLG KETDGSQEPR
PSLKKSHSSP SLHQEEAPTT AKVKRNISER RTYRKIIPKR NRNQL
