PSD1_BOVIN
ID PSD1_BOVIN Reviewed; 1026 AA.
AC F1MUS9; A6QNS4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=PH and SEC7 domain-containing protein 1 {ECO:0000250|UniProtKB:Q5DTT2};
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 {ECO:0000250|UniProtKB:Q5DTT2};
GN Name=PSD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000269|PubMed:19390049};
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI48973.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-1026.
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI48973.1};
RC TISSUE=Fetal brain {ECO:0000312|EMBL:AAI48973.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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. {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 -!- SIMILARITY: Belongs to the PSD family. {ECO:0000255}.
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; AAFC03082941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC148972; AAI48973.1; -; mRNA.
DR RefSeq; NP_001178404.1; NM_001191475.1.
DR AlphaFoldDB; F1MUS9; -.
DR SMR; F1MUS9; -.
DR STRING; 9913.ENSBTAP00000004659; -.
DR PaxDb; F1MUS9; -.
DR PRIDE; F1MUS9; -.
DR GeneID; 523124; -.
DR KEGG; bta:523124; -.
DR CTD; 5662; -.
DR eggNOG; KOG0932; Eukaryota.
DR InParanoid; F1MUS9; -.
DR OrthoDB; 301851at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Coiled coil;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1026
FT /note="PH and SEC7 domain-containing protein 1"
FT /id="PRO_0000411991"
FT DOMAIN 514..708
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 758..871
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 25..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 900..926
FT /evidence="ECO:0000255"
FT COMPBIAS 69..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..366
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTT2"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTT2"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTT2"
FT CONFLICT 155
FT /note="T -> I (in Ref. 2; AAI48973)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="G -> E (in Ref. 2; AAI48973)"
FT /evidence="ECO:0000305"
FT CONFLICT 672..683
FT /note="AETHDLRRLHRY -> GKRMTCGDFIGN (in Ref. 2; AAI48973)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="A -> S (in Ref. 2; AAI48973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1026 AA; 109765 MW; 8B7A4C7574F56C13 CRC64;
MAQGAMRFCS EGDCAISPPR CPRRWLPEGP VPQSPPASMY GSTGSLLRRV AGPGPRSREL
GRVTAPCTPL RGPPSPRIAP SPWAPSSPTG QPPPGARSSV VIFRFVEKAS VRPLNGLPAP
GGLSRSWDLG GVSPPRPTPA LGPGSHQKLR LEASTSDPLP AGGGSARPGT QGLLQGPPTQ
PQVGADGLYS SLPNGLGGPS EHLATLFRGP ADTGLLNQGD IWSSPREVSS HAQRIARAKW
EFFYGSLDPP SSGAKPPEQA PPSPPGVGSG QGSGVAVGRA AKYSETDLDT VPLRCYRETD
IDEVLTEREE ADSAIESQPS SEGLPGTARP PAPRPGPCLG PHPSLGSGNE DEDEAGGEED
VDDEVFEASE GARPGTRMPH SGPLKSPLPF LPGTSPSADG PDSFSCVFEA ILESHRAKGT
SYTSLASLEA LASPGPTQSP FFTFELPPQP PAPRPDPPAP APLAPLEPDS GTSSAADGPW
TQRGEEEEAE AGAKQTPGRD PPSPCHSEDS FGLGAAPLGS EPPLNQLVSD SDSELDSTER
LALGSTDTLS NGQKADLEAA QRLAKRLYRL DGFRKADVAR HLGKNNDFSK LVAGEYLKFF
VFTGMTLDQA LRVFLKELAL MGETQERERV LAHFSQRYFQ CNPGALSSED GAHTLTCALM
LLNTDLHGHN IAETHDLRRL HRYLEGLNEG GDFPRELLKA LYSSIKNEKL QWAIDEEELR
RSLSELADPN PKVIKRVSGG SGSGSSPFLD LTPEPGAAVY KHGALVRKVH ADPDCRKTPR
GKRGWKNFHG ILKGMILYLQ KEEYQPGKAL SEAELKNAIS IHHALATRAS DYSKRPHVFY
LRTADWRVFL FQAPSLEQMQ SWITRINVVA AMFSAPPFPA AVSSQKKFSR PLLPSAATRL
SQEEQVRTHE AKLKAMASEL REHRATQLTK KARGKEAEEQ RQKEAYLEFE KSRYGTYAAL
LRVKLKAGSE ELDAVEAAVA QAGGTEDGLP PPHSSPSLPA NTSSQPRAQC SDSEARAGAG
SGRWKP
