ID A0A287A5A8_PIG Unreviewed; 1514 AA.
AC A0A287A5A8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 3.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Rap guanine nucleotide exchange factor 6 {ECO:0000313|Ensembl:ENSSSCP00000038951.3};
GN Name=RAPGEF6 {ECO:0000313|Ensembl:ENSSSCP00000038951.3,
GN ECO:0000313|VGNC:VGNC:110217};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000038951.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000038951.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000038951.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000038951.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC -!- SIMILARITY: Belongs to the RAPGEF2 family.
CC {ECO:0000256|ARBA:ARBA00010829}.
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DR Ensembl; ENSSSCT00000064186.3; ENSSSCP00000038951.3; ENSSSCG00000014267.5.
DR VGNC; VGNC:110217; RAPGEF6.
DR GeneTree; ENSGT00940000158124; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Bgee; ENSSSCG00000014267; Expressed in mesenteric lymph node and 44 other cell types or tissues.
DR ExpressionAtlas; A0A287A5A8; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01785; RA_PDZ-GEF1; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45161; CYTOSKELETON-ASSOCIATED PROTEIN 4; 1.
DR PANTHER; PTHR45161:SF4; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 6; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 280..380
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 412..526
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 530..600
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 754..840
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 865..1092
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1514 AA; 170056 MW; 9AA47E5311C0B1DE CRC64;
MNSPVDPGAR QALKKKPPER TPEDLNIIYS YLHGMEILSN LREHQLRLMS ARARYERYSG
NQVLFCSETI ARCWYILLSG SVLMKDSMVL PPCSFGKQFG GKRGCDCLVL EPSEMIVVEN
SKDNEDRILQ REIPARQSRR RFRKINYKGE RQTITDDVDI NSYLSLPADL TKMHIADNPH
PQVTHVSSSQ SGCSIASDSG SSSLSDIYQA TESEVGDVDL TRLPEGPVDS EDEEEEDEEI
DRTDPLQGRD LVRECLEKEP ADKTDDDIEQ LLEFMHQLPA FANMTMSVRR ELCSVMIFEV
VEQAGAIILE DGQELDSWYV ILNGTVEISH PDGKVENLFM GNSFGVTPTL DKQYMHGVVR
TKVDDCQFVC IAQQDYWRIL NHVEKNTHKV EEEGEIVMVH EHRELDRSGT RKGHIVIKAT
PERLIMHLIE EHSIVDPTYI EDFLLTYRTF LESPLDVGIK LLEWFKIDSL RDKVTRIVLL
WVNNHFNDFE GDPAMTRFLE EFEKNLEDTK MNGHLRLLNI ACAAKAKWRQ VVLQKASRES
PLHFSLNGGT EKGFGIFVEG VEPSSKAADA GLKRGDQIME VNGQNFENIT FAKALEILRN
NTHLALTVKT NIFVFKELLS RTEQEKSGIP HIPKIAEKKS NRHSIQDVPG DIEQTSQEKG
NKKIKANTVS GGRNKIRKIL DKTRFSILPP KLFSDGGLSQ SQDDSIVGTR HCRHSLAIMP
IPGTLSSSSP DLLQPTTSML DFSNPSAVGF YYIPDQVIRV FKADQQSCYI IISKDTTAKE
VVCQAVHEFG LTGASDTYSL CEVSVTPEGV IKQRRLPDQF SKLADRIQLN GRYYLKNNME
TETLCSDEDA QELVKESQLS MLQLSTIEVA TQLSMRDFDL FRNIEPTEYI DDLFKLDSKT
GNTHLKEFED IVNQETFWVA SEILTESNQL KRMKIIKHFI KIALHCRECK NFNSMFAIIS
GLNLASVARL RGTWEKLPSK YEKHLQDLQD LFDPSRNMAK YRNILSSQSM QPPIIPLFPV
VKKDMTFLHE GNDSKVDGLV NFEKLRMIAK EIRQVVRMTS ANMDPAMMFR QRKKRWRSLG
SLSQGSTNSN MLDVQGGAHK KRARRSSLLN AKKLYEDAQM ARKVKQYLSS LDVETDEEKF
QMMSLQWEPA YGTLTKNLNE KRYVKSSEMS PVPMRSAGQT ARAHLHQPHR VSQVLQVPAV
NLHPIRKKGQ AKDSAMLSTG LPQKVLVTTE EINGKKHTED TISVASSLHS SPPASPQGSP
RKGYTLIPSA KSDNLSDSSH SEISSRSSIV SNCSVDSMSA ALQDERCSSQ AVAAPAPSGA
SEKAEHSSGR GDHSQLGPGW TLSKPSLIKS LAVSSSMSNE EISHEHIIIE AADSGRGSWT
SCSSSSHDNF QSLPNPKGWD FLNSYRHTHL DGPIAEVEPT DFEPYSCPKG CSRTCGQCKG
SPETNQMRQS WASSSSLSDT YEPNYGTVKR RVLENTPAES SEGLDHKDAV DPVYKTVTSS
TEKGLIENEQ VSAV
//
