ID A0A2I0LU16_COLLI Unreviewed; 1618 AA.
AC A0A2I0LU16;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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|EMBL:PKK20909.1};
GN ORFNames=A306_00012791 {ECO:0000313|EMBL:PKK20909.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK20909.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK20909.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK20909.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK20909.1}.
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DR EMBL; AKCR02000096; PKK20909.1; -; Genomic_DNA.
DR RefSeq; XP_013224234.1; XM_013368780.1.
DR STRING; 8932.A0A2I0LU16; -.
DR GeneID; 102086538; -.
DR CTD; 9693; -.
DR InParanoid; A0A2I0LU16; -.
DR OrthoDB; 5473909at2759; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
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; 2.
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: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; 2.
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; 2.
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:UP000053872};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 3..50
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 256..356
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 388..501
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 506..576
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 727..813
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 838..1065
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1618 AA; 181224 MW; 62239AEA2C339D26 CRC64;
MEALSNLREH QLRLMCETVR YERHEANEVL YYPDDIGTCW YILLSGSVFI KESMFLPRSS
FGKRSAGSFR RGCECIVLEP SEMIVVDYMD ENEEYFQRQA SHRQSRRRFR KINQKGERQT
IIDTVDPYPV GKPPLPRGYH TLPADFTKLH LTDSLHPQVT HVSSSHSGCS ITSDSGSSSL
SDIYQATESE AGDMDLSGLP ETAVDSEDDD DEEDIERASD PLMSRDIVRD CLEKDPIDRT
DDDIEQLLEF MHQLPAFANM TMSVRRELCA VMVFAVVERA GTIVLNDGEE LDSWSVILNG
SVEVTYPDGR TEILCMGNSF GVSPTMEKEY MKGVMRTKVD DCQFVCIAQQ DYCRILNQVE
KNMQKVEEEG EIVMVKEHRE LDRTGTRKGH IVIKGTAERL TMHLVEEHSV VDPTFIEDFL
LTYRTFLSSP MEVGKKLLEW FNDPSLRDKV TRVVLLWVNN HFNDFEGDPA MTRFLEEFEN
NLEREKMGGH LRLLNIACAA KAKRRLITLT KPSREAPLPF ILLGGSEKGF GIFVDSVDFG
SKATEAGLKR GDQILEVNGQ NFENIQLSKA MEILRNNTHL SITVKTNLFV FKELLTRLSE
EKRNGAPHLP KIGDIKKASR YSIPDLAVDV EQVIGLEKVN KKSKANTVGG RNKLKKILDK
TRISILPQKP YNDIGIGQSQ DDSIVGLRQS KHIPPALPVS GTLSSSNPDL LQSHHRILDF
NTTPDLPDQV LRVFKADQQS RYIMISKDTT AKEVVIQAIR EFALTTTPDA YSLCEVSVTP
EGVIKQRRLP DQLSKLADRI QLSGRYYLKN NMETETLCSD EDAQELLRES QISLLQLSTV
EVATQLSMRN FELFRNIEPT EYIDDLFKLK SKTGCTNLKM FEEVINQETF WVASEILRET
NQLKRMKIIK HFIKIALHCR ECKNFNSMFA IISGLNLAPV ARLRTTWEKL PSKYEKLFQD
LQDLFDPSRN MAKYRNVLNS QNLQPPIIPL FPVIKKDLTF LHEGNDSKVE GLVNFEKLRM
IAKEIRHVGR MASVNMDPAL MFRTRKKKWR SLGSLSQGST NAAVLDVAQT GGHKKRVRRS
SFLNAKKLYE DAQMARKVKQ YLSNLDLEMD EESLQTLSLQ CEPATNTLPK NTGDKRAGKS
ETSPVAPRAG IQQKVQQQQH KVNQALQVPA VSLYPSRKKV PVKDLPPFGI NSPQALKKIL
SLSEEGSLDR HKKQSEDTIS SASSQLSSPP TSPQSSPRKG YTLAPSGTVD NFSDSGHSEI
SSRSSIVSNS SFDSMPVSLH DERRQRHSVS IVETNLGVGR IDRRIMIEPD QYSLGSYAPL
SETRGLYAGA TVLSSPSTEE LSQDQGDRAS LDAADSGRGS WTSCSSGSHD NIQTIQHQRS
WETLPFGHAH FDSSGDGAGL WASGSHMDQL MFPDHGTKYG RQSQGREGLD QAQSRASWAS
STGYWGEDSE GDTGTIKRRG GKDVSTEAET SSITSVPAEE SKPAPVSTHI AVSSSSTKGL
IARKEGRYRE PPPTPPGYVG IPIAEFAEGG SHPTRKPPDY NIALQRSRMV ARTCETHGTS
TPQQQSHGHS TGRPANKPQW HKPNESDPRL AHYPSQGFST EEDDSGEVKA ANPSSTQM
//