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Database: UniProt
Entry: H3ALX5_LATCH
LinkDB: H3ALX5_LATCH
Original site: H3ALX5_LATCH 
ID   H3ALX5_LATCH            Unreviewed;      1452 AA.
AC   H3ALX5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Rap guanine nucleotide exchange factor 2 {ECO:0000256|ARBA:ARBA00016709};
DE   AltName: Full=Cyclic nucleotide ras GEF {ECO:0000256|ARBA:ARBA00031545};
DE   AltName: Full=Neural RAP guanine nucleotide exchange protein {ECO:0000256|ARBA:ARBA00032021};
DE   AltName: Full=PDZ domain-containing guanine nucleotide exchange factor 1 {ECO:0000256|ARBA:ARBA00030673};
DE   AltName: Full=RA-GEF-1 {ECO:0000256|ARBA:ARBA00029925};
DE   AltName: Full=Ras/Rap1-associating GEF-1 {ECO:0000256|ARBA:ARBA00031980};
GN   Name=RAPGEF2 {ECO:0000313|Ensembl:ENSLACP00000010646.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000010646.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000010646.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC       Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, perinuclear
CC       region {ECO:0000256|ARBA:ARBA00004556}. Endosome
CC       {ECO:0000256|ARBA:ARBA00004177}. Late endosome
CC       {ECO:0000256|ARBA:ARBA00004603}.
CC   -!- SIMILARITY: Belongs to the RAPGEF2 family.
CC       {ECO:0000256|ARBA:ARBA00010829}.
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DR   EMBL; AFYH01113660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01113661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01113662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01113663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSLACT00000010725.1; ENSLACP00000010646.1; ENSLACG00000009378.2.
DR   GeneTree; ENSGT00940000156418; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000009378; Expressed in post-anal tail muscle and 6 other cell types or tissues.
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; 1.
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:SF2; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 2; 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; 1.
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 junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
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:UP000008672};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          63..163
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          195..309
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50212"
FT   DOMAIN          313..383
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          539..624
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          649..876
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          995..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1177..1211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1275..1358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1401..1452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..24
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..986
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1083
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1293..1307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1310..1339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1452 AA;  162468 MW;  5CC9F693B59976BC CRC64;
     MDLSGLPETA VDSEDDDDEE DIERASDPLM SRDVVRDCLE KDPIDRTDDD IEQLLEFMHQ
     LPAFANMTMS VRKELCAVMV FAVVERAGTI VLNDGEELDS WSVILNGSVE VTYPDGRTEI
     LCMGNSFGVS PTMEKEYMKG VMKTKVDDCQ FVCIAQQDYC RILNQVEKNM QKVEEEGEIV
     MVKEHRELDR TGTRKGHIVI KGTPERLTMH LVEEHSVVDP TFIEDFLLTY RTFLSSPMEV
     GKKLLEWFND PSLRDKVTRV VLLWVNNHFN DFEGDTAMTR FLEEFENSLE REKMMGHLRL
     LNIACAAKAK RRLITLTKPS REAPLPFILL GGSEKGLGIF VDSVESGSKA AETGLKRGDR
     ILEVNGQNFE NVQLSKAMEI LKNNTHLSIT VKTNLFEFKQ LLTRLAEEKR NGAPHLPKIG
     DIKKASRYSI PDLAVDVEQV MGLEKVNKKS KANTVGGKNK LKKIFDKTRI SILPQKPYND
     IGIGQSQDDS IVGLRQSKHI PPTLPVSGNL SSSNPDLLQS HHRILDFNNS PAAGFYNLPD
     QVLRVFKADQ QSRYIMISKD TTAKEVVHQA LREFALTGPE NYSLCEVSVT PEGVIKQKRL
     PDQLSKLADK IQLSGRYYLK NNMETETLCS DEDAQELLKE SQISLLQLST IEVATQLSMR
     NFELFRNIEA TEYIDDLFKL KTKVGSSNLK KFEEVINQET FWVASEILKE LNQIKRMKII
     KHFIKIALHC RECKNFNSMF AIISGLNLAP VARLRSTWEK LNSKYEKLFQ DLQDLFDPSR
     NMAKYRNVLN SQNLQPPIIP LFPVIKKDLT FLHEGNDSKV EGLVNFEKLR MIAKEIRHVG
     RMASVNMDPA LMFRTRKKKW RSLGSLSQGS TNAALDVVQT GGHKKRVRRS SFLNAKKLYE
     DAQMARKVKQ YLANLVLEMD EDSLQVLSLV CEPSTNTLPK NAGDRRSGKC DTSPVTPRAG
     TQQPKTQQPQ PQQQQPQQQQ QKGNQALQVP PVSLYPSRKK VPVKDLPPFG TSSPQALRKI
     LSLSEEANFD RHKKQAEDTI SNASSQLSSP PTSPQTSPRK GGSQLRSHGS RHSDLTGSSS
     SLGSYTLAPS GTVDNFSDSG HSEISSRSSI VSNSSFDCVP MHDEKRQRHS VSIVEANLGV
     GRIDRRAVMD PDQYSFSSYS PVPENRSLYA GATVLSSPST EELTQDQGDR ASLDAADSGR
     GSWTSCSSGS HDNIQTIQHQ RSWETLAFGH THFDSAAEGA ALWASGNHMD QLMFSELANK
     CSRYSQAREN LDQAQSRGSW ASSPGYWGEE TEGDTGTIKR RGGKDVAAEA ETSSITSLTS
     EESKNIRPSH ITVSSSTAKG LIARKEGRYR EPPPTPPGYI GIPIADFPEV SSFQTRKPPD
     YNVALQRSRF VARPCEPLGA SATQQLHGHP AARTVNKPQW HRPNESDPRL ALYQSQGFSA
     EEEDEDEQVS AV
//
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