ID A0A2K5JZL1_COLAP Unreviewed; 1391 AA.
AC A0A2K5JZL1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Rap guanine nucleotide exchange factor 6 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000034257.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000034257.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
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DR RefSeq; XP_011806432.1; XM_011951042.1.
DR Ensembl; ENSCANT00000057487.1; ENSCANP00000034257.1; ENSCANG00000040763.1.
DR GeneID; 105518172; -.
DR CTD; 51735; -.
DR OrthoDB; 5473909at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005737; C: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: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 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 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 4: Predicted;
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080}.
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 749..835
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 860..1088
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 157525 MW; 2D37B4C5FBF1C90C CRC64;
MNSPVDPGAR QALRKKPPER TPEDLNTIYS YLHGMEILSN LREHQLRLMS ARARYERYSG
NQVLFCSETI ARCWYILLSG SVLVKGSMVL PPCSFGKQFG GKRGCDCLVL EPSEMIVVEN
AKDNEDSILQ REIPARQSRR RFRKINYKGE RQTITDDVEV NSYLSLPADL TKMHLTDNPH
PQVTHVSSSQ SGCSIASDSG SSSLSDIYQA TESEVGDVDL TRLPEGPVDS EDDEEEDEEI
DRTDPLQGRD LVRECLEKEP ADKTDDDIEQ LLEFMHQLPA FANMTMSVRR ELCSVMIFEV
VEQAGAIILE DGQELDSWYV ILNGTVEISH PDGKVENLFM GNSFGITPTL DKQYMHGIVR
TKVDDCQFVC IAQQDYWRIL NHVEKNTHKV EEEGEIVMVH EHRELDRSGT RKGHIVIKAT
PERLIMHLIE EHSIVDPTYI EDFLLTYRTF LESPLDVGIK LLEWFKIDSL RDKVTRIVLL
WVNNHFNDFE GDPAMTRFLE EFEKNLEDTK MNGHLRLLNI ACAAKAKWRQ VVLQKASRES
PLQFSLNGGS EKGFGIFVEV VEPGSKAADS GLKRGDQIME VNGQNFENIT FMKALEILRN
NTHLALTVKT NIFVFKELLF RTEQEKSGVP HIPKIAEKKS NRHSIQHVPG DIEQTSQEKG
SKKVKANTVS GGRNKIRKIL DKTRFSILPP KLFSDGGLSQ SQDDSIVGTR HCRHSLAIMP
IPGTLSSSSP DLLQPTTSML DFSNPSDIPD QVIRVFKVDQ QSCYIIISKD TTAKEVVCHA
VHEFGLTGAS DTYSLCEVSV TPEGVIKQRR LPDQFSKLAD RIQLNGRYYL KNNMETETLC
SDEDAQELVK ESQLSMLQLS TIEVATQLSM RDFDLFRNIE PTEYIDDLFK LNSKTGNTHL
KRFEDIVNQE TFWVASEILT EANQLKRMKI IKHFIKIALH CRECKNFNSM FAIISGLNLA
SVARLRGTWE KLPSKYEKHL QDLQDIFDPS RNMAKYRNIL SSQSMQPPII PLFPVVKKDM
TFLHEGNDSK VDGLVNFEKL RMISKEIRQV VRMTSANMDP AMMFRQRSLS QGSTNSNMLD
VQGGAHKKRA RRSSLLNAKK LYEDAQMARK VKQYLSSLDV ETDEEKFQMM SLQWEPAYGT
LTKNLSEKRS AKSSEMSPVP MRSAGQTTKA HLHQPHRVSQ VLQVPAVNLH PIRKKGQTKD
PALSTSLPQK VLGTTEEVSG KKHTEDTISV ASSLHSSPPA SPQVSPHKVG SIICDHSSKI
SGQSCPGIGG AYLQKKILQI TRSTAKRTDS TEKATEVNRD RTSCENTTRK RMTSPFRRLR
ERMLSRERLV NSQKEDTDHN QATESCEKVK DVGSNIKDEK GSAIFNSNSQ GNSNTLNCFY
TRFKSKRRKT L
//
