PSD1_RAT
ID PSD1_RAT Reviewed; 649 AA.
AC Q9ESQ7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=PH and SEC7 domain-containing protein 1;
DE AltName: Full=Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6;
DE Short=Exchange factor for ARF6;
DE AltName: Full=Exchange factor for ARF6 A;
DE AltName: Full=Pleckstrin homology and SEC7 domain-containing protein 1;
GN Name=Psd; Synonyms=Efa6, Psd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=11834294; DOI=10.1016/s0169-328x(01)00312-6;
RA Suzuki I., Owada Y., Suzuki R., Yoshimoto T., Kondo H.;
RT "Localization of mRNAs for subfamily of guanine nucleotide-exchange
RT proteins (GEP) for ARFs (ADP-ribosylation factors) in the brain of
RT developing and mature rats under normal and postaxotomy conditions.";
RL Brain Res. Mol. Brain Res. 98:41-50(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Guanine nucleotide exchange factor for ARF6 (By similarity).
CC Induces cytoskeletal remodeling (By similarity).
CC {ECO:0000250|UniProtKB:A5PKW4, ECO:0000250|UniProtKB:Q5DTT2}.
CC -!- SUBUNIT: Interacts with ACTN1. Interacts (ARF6-bound form) with KCNK1;
CC does not interact with KCNK1 in the absence of ARF6 (By similarity).
CC {ECO:0000250|UniProtKB:Q5DTT2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A5PKW4}.
CC Cell projection, ruffle membrane {ECO:0000250|UniProtKB:A5PKW4}.
CC Cleavage furrow {ECO:0000250|UniProtKB:A5PKW4}. Note=Distributed
CC uniformly on the plasma membrane, as well as throughout the cytoplasm
CC during metaphase. Subsequently concentrated at patches in the
CC equatorial region at the onset of cytokinesis, and becomes distributed
CC in the equatorial region concurrent with cleavage furrow ingression. In
CC later cytokinesis phases, fades away from the cleavage furrow and
CC becomes uniformly distributed throughout the plasma membrane.
CC {ECO:0000250|UniProtKB:A5PKW4}.
CC -!- TISSUE SPECIFICITY: Brain. Expressed in the hippocampal and dentate
CC neuronal layers, cerebellar cortex, molecular layer of the hippocampus
CC and dentate gyrus. {ECO:0000269|PubMed:11834294}.
CC -!- DEVELOPMENTAL STAGE: On embryonic day 15 (E15) and E18, weakly
CC expressed in the mantle zone throughout the neuraxis. On postnatal days
CC 0 (P0) and P7, expression is evident in the cerebral neocortex,
CC hippocampal pyramidal and dentate granule cell layers, olfactory
CC granule, mitral cell layers and the striatum. A weak expression is seen
CC in the gray matter of di-, mes- and met-encephalon and in the
CC cerebellar Purkinje cells. On P14, expressed in the gray matter of the
CC telencephalon such as the cerebral neocortex, olfactory bulb,
CC hippocampus, dentate gyrus and striatum. On P21 and thereafter detected
CC in the cerebellar granule cells. {ECO:0000269|PubMed:11834294}.
CC -!- SIMILARITY: Belongs to the PSD family. {ECO:0000305}.
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DR EMBL; AB040468; BAB12573.1; -; mRNA.
DR RefSeq; XP_017444225.1; XM_017588736.1.
DR AlphaFoldDB; Q9ESQ7; -.
DR SMR; Q9ESQ7; -.
DR STRING; 10116.ENSRNOP00000026378; -.
DR iPTMnet; Q9ESQ7; -.
DR PhosphoSitePlus; Q9ESQ7; -.
DR PaxDb; Q9ESQ7; -.
DR PRIDE; Q9ESQ7; -.
DR GeneID; 171381; -.
DR UCSC; RGD:620297; rat.
DR CTD; 5662; -.
DR RGD; 620297; Psd.
DR eggNOG; KOG0932; Eukaryota.
DR InParanoid; Q9ESQ7; -.
DR PhylomeDB; Q9ESQ7; -.
DR PRO; PR:Q9ESQ7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0098999; C:extrinsic component of postsynaptic endosome membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0001409; F:guanine nucleotide transmembrane transporter activity; TAS:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0015854; P:guanine transport; TAS:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
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; IPR001605; PH_dom-spectrin-type.
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 PRINTS; PR00683; SPECTRINPH.
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; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..649
FT /note="PH and SEC7 domain-containing protein 1"
FT /id="PRO_0000318299"
FT DOMAIN 137..331
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 381..494
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 523..549
FT /evidence="ECO:0000255"
FT COILED 581..608
FT /evidence="ECO:0000255"
FT COMPBIAS 64..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 649 AA; 70818 MW; 52F7D37C3F5DA8C2 CRC64;
MPHSGLLKSP VPFLPGTSPS ADGPDSFSCM FEAIMESHRA KGTSYSSLAS LEALASPGPT
QSPFFTFEMP PQPPAPRPDP PAPAPLAPLE PDSGTSSVAD GPWTQRREVE ESDAGATLAP
RKELPSPSHS EDSLGLGAAP LGSEPPLSQL VSDSDSELDS TERLALGSTD TLSNGQKADL
EAAQRLAKRL YRLDGFRKAD VARHLGKNND FSKLVAGEYL KFFVFTGMTL DQALRVFLKE
LALMGETQER ERVLAHFSQR YFQCNPEALS SEDGAHTLTC ALMLLNTDLH GHNIGKRMTC
GDFIGNLEGL NDGGDFPREL LKALYSSIKN EKLQWAIDEE ELRRSLSELA DPNPKVIKRV
SGGSGSSSSP FLDLTPEPGA AVYKHGALVR KVHADPDCRK TPRGKRGWKS FHGILKGMIL
YLQKEEYQPG KALSEAELKN AISIHHALAT RASDYSKRPH VFYLRTADWR VFLFQAPSLE
QMQSWITRIN VVAAMFSAPP FPAAVSSQKK FSRPLLPSAA TRLSQEEQVR THEAKLKAMA
SELREHRAAH LGKKARGKEA EEQRQKETYL EFEKSRYGTY AALLRVKMKA ASEELDAIEA
ALAQAGSTEE GCPPPHSSPS LQPNPTSQPR AQRPGSEARA GAGSTRPKP
