RBG1L_PONAB
ID RBG1L_PONAB Reviewed; 815 AA.
AC Q5RCW6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Rab GTPase-activating protein 1-like;
GN Name=RABGAP1L {ECO:0000250|UniProtKB:Q5R372};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH90391.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart {ECO:0000312|EMBL:CAH90391.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTP-hydrolysis activating protein (GAP) for small GTPase
CC RAB22A, converting active RAB22A-GTP to the inactive form RAB22A-GDP
CC (By similarity). Plays a role in endocytosis and intracellular protein
CC transport. Recruited by ANK2 to phosphatidylinositol 3-phosphate
CC (PI3P)-positive early endosomes, where it inactivates RAB22A, and
CC promotes polarized trafficking to the leading edge of the migrating
CC cells. Part of the ANK2/RABGAP1L complex which is required for the
CC polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma
CC membrane that enables continuous directional cell migration (By
CC similarity). {ECO:0000250|UniProtKB:A6H6A9,
CC ECO:0000250|UniProtKB:Q5R372}.
CC -!- SUBUNIT: Interacts (via Rab-GAP TBC domain) with ANK2 (via death
CC domain). {ECO:0000250|UniProtKB:Q5R372}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q5R372}.
CC Golgi apparatus {ECO:0000250|UniProtKB:Q5R372}. Note=Colocalizes on
CC endosomes partially with EEA1 (By similarity). Colocalizes and
CC cotransports on motile vesicles with ANK2 (By similarity).
CC {ECO:0000250|UniProtKB:A6H6A9, ECO:0000250|UniProtKB:Q5R372}.
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
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DR EMBL; CR858152; CAH90391.1; -; mRNA.
DR RefSeq; NP_001125191.1; NM_001131719.2.
DR AlphaFoldDB; Q5RCW6; -.
DR SMR; Q5RCW6; -.
DR STRING; 9601.ENSPPYP00000000563; -.
DR Ensembl; ENSPPYT00000000586; ENSPPYP00000000563; ENSPPYG00000000487.
DR GeneID; 100172082; -.
DR KEGG; pon:100172082; -.
DR CTD; 9910; -.
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000154611; -.
DR InParanoid; Q5RCW6; -.
DR OrthoDB; 191811at2759; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0090630; P:activation of GTPase activity; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR042809; RABGAP1L.
DR PANTHER; PTHR22957:SF205; PTHR22957:SF205; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 2: Evidence at transcript level;
KW Endocytosis; Endosome; Golgi apparatus; GTPase activation; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..815
FT /note="Rab GTPase-activating protein 1-like"
FT /id="PRO_0000348056"
FT DOMAIN 126..282
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 538..724
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 580
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 621
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5R372"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5R372"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5R372"
SQ SEQUENCE 815 AA; 92569 MW; F14748EB20085CE8 CRC64;
MEVRASLQKV SGSSDSVATM NSEEFVLVPQ YADDNSTKHE EKPQLKIVSN GDEQLEKAME
EILRDSEKRQ SSLLVDCQSS SEISDHSFGD IPASQTNKPS LQLILDPSNT EISTPRPSSP
GGLPEEDSVL FNKLTYLGCM KVSSPRNEVE ALRAMATMKS SSQYPFPVTL YVPNVPEGSV
RIIDQSSNVE IASFPIYKVL FCARGHDGTT ESNCFAFTES SHGSEEFQIH VFSCEIKEAV
SRILYSFCTA FKRSSRQVSD VKDSVIPTPD SDVFTFSVSL EVKEDDGKGN FSPVPKDRDK
FYFKLKQGIE KKVVITVQQL SNKELAIERC FGMLLSPGRN VKNSDMHLLD MESMGKSYDG
RAYVITGMWN PNAPIFLALN EETPKDKRVY MTVAVDMVVT EVVEPVRFLL ETVVRVYPAN
ERFWYFSRKT FTETFFMRLK QSQGKGHTNA GDAIYEVVSL QRESDKEEPV TPTSGGGPMS
PQDDEAEEES DNELSSGTGD VSKDCPEKIL YSWGELLGKW HSNLGARPKG LSTLVKSGVP
EALRAEVWQL LAGCHDNQAM LDRYRILITK DSAQESVITR DIHRTFPAHD YFKDTGGDGQ
ESLYKICKAY SVYDEDIGYC QGQSFLAAVL LLHMPEEQAF CVLVKIMYDY GLRDLYKNNF
EDLHCKFYQL ERLMQEQLPD LHSHFSDLNL EAHMYASQWF LTLFTAKFPL CMVFHIIDLL
LCEGLNIIFH VALALLKTSK EDLLQADFEG ALKFFRVQLP KRYRAEENAR RLMEQACNIK
VPIKKLKKYE KEYQTMRESQ LQQEDPMDRY KFVYL
