TBD2A_RAT
ID TBD2A_RAT Reviewed; 924 AA.
AC B5DFA1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=TBC1 domain family member 2A;
GN Name=Tbc1d2; Synonyms=Tbc1d2a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acts as GTPase-activating protein for RAB7A. Signal effector
CC acting as a linker between RAC1 and RAB7A, leading to RAB7A
CC inactivation and subsequent inhibition of cadherin degradation and
CC reduced cell-cell adhesion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with activated RAC1 and CDH1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Cell junction {ECO:0000250}.
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DR EMBL; BC168982; AAI68982.1; -; mRNA.
DR RefSeq; XP_006238118.1; XM_006238056.3.
DR AlphaFoldDB; B5DFA1; -.
DR SMR; B5DFA1; -.
DR STRING; 10116.ENSRNOP00000011714; -.
DR PaxDb; B5DFA1; -.
DR PeptideAtlas; B5DFA1; -.
DR PRIDE; B5DFA1; -.
DR Ensembl; ENSRNOT00000011714; ENSRNOP00000011714; ENSRNOG00000023348.
DR GeneID; 313234; -.
DR UCSC; RGD:1306860; rat.
DR CTD; 55357; -.
DR RGD; 1306860; Tbc1d2.
DR eggNOG; KOG2058; Eukaryota.
DR GeneTree; ENSGT00940000159937; -.
DR HOGENOM; CLU_011278_0_0_1; -.
DR InParanoid; B5DFA1; -.
DR OMA; KTICNSR; -.
DR OrthoDB; 1162786at2759; -.
DR PhylomeDB; B5DFA1; -.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR PRO; PR:B5DFA1; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000023348; Expressed in liver and 18 other tissues.
DR ExpressionAtlas; B5DFA1; baseline and differential.
DR Genevisible; B5DFA1; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..924
FT /note="TBC1 domain family member 2A"
FT /id="PRO_0000395195"
FT DOMAIN 42..140
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 621..813
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..167
FT /note="Interaction with CADH1"
FT /evidence="ECO:0000250"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..435
FT /note="Interaction with RAC1"
FT /evidence="ECO:0000250"
FT COILED 303..332
FT /evidence="ECO:0000255"
FT COILED 361..418
FT /evidence="ECO:0000255"
FT COILED 444..477
FT /evidence="ECO:0000255"
FT COILED 871..906
FT /evidence="ECO:0000255"
FT COMPBIAS 228..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYX2"
SQ SEQUENCE 924 AA; 104975 MW; 4B975CFCE255B06C CRC64;
MEDTPERTPS SESIQPPGLA REPEVTSPGD SEGCARPLDP APKKLCGYLS KFGGKGPIKG
WKCRWFFYDE RKCHLYYSRT AQDANPLDSI DLSSATFDCK ADAEEEGTFE IKTPSRVITL
KAATRQVMLY WLQQLQMKRW EFHNSPPALP ATPAAALTEN GPTLHLKLEQ EEAELEEFLC
PVKTPPGLVG TAAALQPVPA MPSALQNISL KHLGTEIQNT MYNIRGNKQA QATAHGPPVE
ESSQSAEPQR GEQPLISDPS IPEKEPEDPP KSAPRSCVPS GPMQKPKRQS NTFPFFSDGL
ARSRTAQEKV VALEQQVLML TKELKSQKEL VIILHKALEA AQQEKRASSA YLAATEDRDR
LELVRHKVRQ IAELNQRVEA LEQDRERLVH EAGLREQQVQ ALQQHVQLLM DKNQAKQQVI
CKLSQKLTED LAQPQPADAT NGDFLSQQER LEHLKDDMEA YRTQNRFLNS EIHQVTKIWR
KVAEKEKALL TKCAYLQARN CQVESKYLAG LRRLQEAAGA EPGDFPELLQ QLVQEALQWE
AGEASDSVGL SPVSEYDDYG FLTVPDYEVE DLKLLAKIQA LEVRSHHLLA LEAVERPLRD
RWATLTELMP SAELKQLLRA GVPREHRPRV WRWLVHRRVQ HLHSSGCYQE LLARGRACEH
PAARQIELDL NRTFPTNKHF TCPTSSFPDK LRRVLLAFSW QNPTIGYCQG LNRLAAIALL
VLEDEESAFW CLVAIVETIL PAEYYSKTLT ASQVDQRVLQ DLLSEKLPRL TAHLGQRHVD
LSLITFNWFL VIFADSLISD ILLRVWDAFL YEGTKVVFRY ALAIFKYNEE AILRLQDSLE
IYQYLRFFTK TICDSRKLTS IAFNDMNPFP MKQLRQLRAA HRERLEAELR ELELLKAEYL
ERRASRGRAV PEGCVSEDEG EGDS
