TBD2A_MOUSE
ID TBD2A_MOUSE Reviewed; 922 AA.
AC B1AVH7; Q3UFW9; Q8BYB1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=TBC1 domain family member 2A;
GN Name=Tbc1d2; Synonyms=Tbc1d2a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-773 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B1AVH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B1AVH7-2; Sequence=VSP_039384;
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DR EMBL; AK041359; BAC30918.1; -; mRNA.
DR EMBL; AK148254; BAE28440.1; -; mRNA.
DR EMBL; AL683884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX571848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX682536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18155.1; -. [B1AVH7-1]
DR RefSeq; NP_941066.3; NM_198664.3. [B1AVH7-1]
DR AlphaFoldDB; B1AVH7; -.
DR SMR; B1AVH7; -.
DR STRING; 10090.ENSMUSP00000081670; -.
DR iPTMnet; B1AVH7; -.
DR PhosphoSitePlus; B1AVH7; -.
DR EPD; B1AVH7; -.
DR MaxQB; B1AVH7; -.
DR PaxDb; B1AVH7; -.
DR PeptideAtlas; B1AVH7; -.
DR PRIDE; B1AVH7; -.
DR ProteomicsDB; 263079; -. [B1AVH7-1]
DR ProteomicsDB; 263080; -. [B1AVH7-2]
DR Antibodypedia; 28952; 107 antibodies from 23 providers.
DR Ensembl; ENSMUST00000084621; ENSMUSP00000081670; ENSMUSG00000039813. [B1AVH7-1]
DR Ensembl; ENSMUST00000107750; ENSMUSP00000103379; ENSMUSG00000039813. [B1AVH7-2]
DR GeneID; 381605; -.
DR KEGG; mmu:381605; -.
DR UCSC; uc008suf.1; mouse. [B1AVH7-1]
DR CTD; 55357; -.
DR MGI; MGI:2652885; Tbc1d2.
DR VEuPathDB; HostDB:ENSMUSG00000039813; -.
DR eggNOG; KOG2058; Eukaryota.
DR GeneTree; ENSGT00940000159937; -.
DR HOGENOM; CLU_011278_0_0_1; -.
DR InParanoid; B1AVH7; -.
DR OMA; KTICNSR; -.
DR OrthoDB; 1162786at2759; -.
DR PhylomeDB; B1AVH7; -.
DR TreeFam; TF317336; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 381605; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Tbc1d2; mouse.
DR PRO; PR:B1AVH7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AVH7; protein.
DR Bgee; ENSMUSG00000039813; Expressed in granulocyte and 72 other tissues.
DR Genevisible; B1AVH7; MM.
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; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
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 Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..922
FT /note="TBC1 domain family member 2A"
FT /id="PRO_0000395194"
FT DOMAIN 43..141
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 619..811
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..168
FT /note="Interaction with CADH1"
FT /evidence="ECO:0000250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..435
FT /note="Interaction with RAC1"
FT /evidence="ECO:0000250"
FT COILED 302..333
FT /evidence="ECO:0000255"
FT COILED 362..417
FT /evidence="ECO:0000255"
FT COILED 443..476
FT /evidence="ECO:0000255"
FT COILED 869..904
FT /evidence="ECO:0000255"
FT COMPBIAS 277..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYX2"
FT VAR_SEQ 220..922
FT /note="NTMHNIRGNKQAQAAAHGPLVEDSPQGGEPQSGEQPSISDPSLPEKEPEDPA
FT KSAPRSSVPSGPTQKPKRQSNTFPFFSDGLARSRTAQEKVAALEQQVLMLTKELKSQKE
FT LVIILHKALEAAQQEKRASSAYLAATEDRDRLELVRHKVRQIAELNQRVEALEQGRERL
FT AHEAGLREQQVQALQQHVQLLMDKNHAKQQVICKLTQKLTEDLAQPADATNGDFLSQQE
FT RMEHLKDDMEAYRTQNRFLNSEIHQVTKIWRKVAEKEKALLTKCAYLQARNCQVESKYL
FT AGLRRLQEAAGAEAGDFPELLQQLIQEALQWEAGEADSVGLSPVSEYDDYGFLTVPDYE
FT MEDLKLLAKIQALEVRSHHLLAHEAVERPLRDRWATLTELTPSAELKQLLRAGVPREHR
FT PRVWRWLVHRRVRHLQAPGCYQELLARGRACEHPAARQIELDLNRTFPTNKHFTCPTSS
FT FPDKLRRVLLAFSWQNPTIGYCQGLNRLAAIALLVLEDEESAFWCLVAIVETILPAEYY
FT SKTLTASQVDQRVLQDLLSEKLPRLTAHLGQHRVDLSLITFNWFLVVFADSLISDILLR
FT VWDAFLYEGTKVVFRYALAIFKYNEEAILQLQDSLEIYQYLRFFTKTICDSRKLMSIAF
FT NDMNPFPMKQLRQLRAAHRERLEAELRELELLKVEYLQRRASLGRAPPEGCVSEDEGEG
FT DS -> AVGVVTSTGAGVQETWSNTFHPM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039384"
FT CONFLICT 27
FT /note="V -> A (in Ref. 1; BAE28440)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="A -> T (in Ref. 1; BAE28440)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="L -> P (in Ref. 1; BAE28440)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="V -> M (in Ref. 1; BAE28440)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="S -> L (in Ref. 1; BAE28440)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="H -> Q (in Ref. 1; BAE28440)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="E -> G (in Ref. 1; BAE28440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 922 AA; 104260 MW; 729C466D976B8C8E CRC64;
MEDAPERTPS SSESTQPPGL AREPEVVSPG DSEGCARPLD TVPKKLCGYL SKFGGKGPIK
GWKCRWFFYD ERKCHLYYSR TAQDANPLDS IDLSSAVFDC KADAEEEGTF EIKTPSRVIT
LKAATKQAML YWLQQLQMKR WEFHNSPPAL PATPAAALAE NGPTLHLKLE QEEAELEEFL
CPVKTPTGLV GAAAALQPVP AVPSALQNIS LKHLGTEIQN TMHNIRGNKQ AQAAAHGPLV
EDSPQGGEPQ SGEQPSISDP SLPEKEPEDP AKSAPRSSVP SGPTQKPKRQ SNTFPFFSDG
LARSRTAQEK VAALEQQVLM LTKELKSQKE LVIILHKALE AAQQEKRASS AYLAATEDRD
RLELVRHKVR QIAELNQRVE ALEQGRERLA HEAGLREQQV QALQQHVQLL MDKNHAKQQV
ICKLTQKLTE DLAQPADATN GDFLSQQERM EHLKDDMEAY RTQNRFLNSE IHQVTKIWRK
VAEKEKALLT KCAYLQARNC QVESKYLAGL RRLQEAAGAE AGDFPELLQQ LIQEALQWEA
GEADSVGLSP VSEYDDYGFL TVPDYEMEDL KLLAKIQALE VRSHHLLAHE AVERPLRDRW
ATLTELTPSA ELKQLLRAGV PREHRPRVWR WLVHRRVRHL QAPGCYQELL ARGRACEHPA
ARQIELDLNR TFPTNKHFTC PTSSFPDKLR RVLLAFSWQN PTIGYCQGLN RLAAIALLVL
EDEESAFWCL VAIVETILPA EYYSKTLTAS QVDQRVLQDL LSEKLPRLTA HLGQHRVDLS
LITFNWFLVV FADSLISDIL LRVWDAFLYE GTKVVFRYAL AIFKYNEEAI LQLQDSLEIY
QYLRFFTKTI CDSRKLMSIA FNDMNPFPMK QLRQLRAAHR ERLEAELREL ELLKVEYLQR
RASLGRAPPE GCVSEDEGEG DS
