RBG1L_CHICK
ID RBG1L_CHICK Reviewed; 816 AA.
AC Q5ZJ17;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Rab GTPase-activating protein 1-like;
GN Name=RABGAP1L {ECO:0000250|UniProtKB:Q5R372}; ORFNames=RCJMB04_21k9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|EMBL:CAG32276.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG32276.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG32276.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 with ANK2. {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; AJ720617; CAG32276.1; -; mRNA.
DR RefSeq; NP_001012941.1; NM_001012923.1.
DR AlphaFoldDB; Q5ZJ17; -.
DR SMR; Q5ZJ17; -.
DR STRING; 9031.ENSGALP00000007275; -.
DR PaxDb; Q5ZJ17; -.
DR GeneID; 424438; -.
DR KEGG; gga:424438; -.
DR CTD; 9910; -.
DR VEuPathDB; HostDB:geneid_424438; -.
DR eggNOG; KOG1102; Eukaryota.
DR InParanoid; Q5ZJ17; -.
DR PhylomeDB; Q5ZJ17; -.
DR PRO; PR:Q5ZJ17; -.
DR Proteomes; UP000000539; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
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;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..816
FT /note="Rab GTPase-activating protein 1-like"
FT /id="PRO_0000348057"
FT DOMAIN 125..281
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 539..725
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 29..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 581
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 622
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
SQ SEQUENCE 816 AA; 92566 MW; B6A3CA0B625A65DD CRC64;
MEVRTSFSKA RRIPEAVSTL INEEFVVVHQ QTEDSSGKDA KPQLKVFSNG DDQLEKAMEE
ILRDSEKDQN NSTALPEGSS DACSQASGLG SGGQTNQPSL QLVLDPSTTE VSARRSSSPS
EPLEEDSVLF NKLTYLGSMK VSAPRNEPEA LRAMANMKSS SQAPLSVTLY VPNVPEGSVR
IIDQSSNVEI ASFPIYKVLF CVRGQNGTSE SDCFAFTESS CGTEEFQIHV FSCEIKEAVS
RILYSFSTAF KRSSKQASDH VKDFVLHTPD SDVYTFSVSL EVKEDDGKGN FSPVPKDRDK
LYFKLKQGIE KKVVITVQQL SNKELAIERC FGMLLSPGRN VKNSDMHLLD MESMGKSSDG
KAYVITGIWN PNAPMFLVLN EETPKDKRVY MTVAVDMVVT EVVEPVRFLL ETVVRVYPAN
ERFWYFSRKT FTETFYMKLK QSEGKSHTSA GDPIYEVASL QRESAREEQL LSPTSGGGPV
SSQEDEAEEE SDNELSSGTG DVSKDCPEKI LYSWGELLGR WHNNLVVRPN GLSTLVKRGV
PEALRAEVWQ LLAGCHDNEA MLDKYRILIT MDSAQENVIT RDIHRTFPAH DYFKDTEGDG
QESLYKICKA YSVYDEDIGY CQGQSFLAAV LLLHMPEEQA FCVFVKIMYD YGLRDLYRNN
FEDLHCKFFQ LEKLMQEQLP DLYSHFSDLN LEAHMYASQW FLTLFTAKFP LCMVFHIIDL
LLCEGMNIIF HVALALLKTS KEDLLQADFE GALKFFRVQL PKRYRAEENA RRLMEQACNI
KVPTKKLKKY EREYQTMRES QLQQEDPMDR YKFICL
