TBD2A_AILME
ID TBD2A_AILME Reviewed; 923 AA.
AC D2H0G5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=TBC1 domain family member 2A;
GN Name=TBC1D2; Synonyms=TBC1D2A; ORFNames=PANDA_002915;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Cell junction {ECO:0000250}.
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DR EMBL; GL192407; EFB16841.1; -; Genomic_DNA.
DR AlphaFoldDB; D2H0G5; -.
DR SMR; D2H0G5; -.
DR STRING; 9646.ENSAMEP00000004867; -.
DR eggNOG; KOG2058; Eukaryota.
DR HOGENOM; CLU_011278_0_0_1; -.
DR InParanoid; D2H0G5; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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:0005096; F:GTPase activator activity; ISS:UniProtKB.
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 3: Inferred from homology;
KW Acetylation; Cell junction; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..923
FT /note="TBC1 domain family member 2A"
FT /id="PRO_0000395192"
FT DOMAIN 47..144
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 631..823
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..171
FT /note="Interaction with CADH1"
FT /evidence="ECO:0000250"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..439
FT /note="Interaction with RAC1"
FT /evidence="ECO:0000250"
FT REGION 900..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 308..486
FT /evidence="ECO:0000255"
FT COILED 870..904
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYX2"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYX2"
SQ SEQUENCE 923 AA; 104425 MW; FC51459DA10BF9C0 CRC64;
MDGAHENAAE SSSSVPRSEE PACSAGGPEV LPPEESEGCA GSLDAAPKKL CGYLSKFGGK
GPIRGWKSRW FFYDERKCHL YYSRTAQDAN PLDSIDLSSA VFDCKADAEE GTFEIKTPSR
IITLKAATKQ VMLYWLQQLQ TKRWEFHSSP PAPPAAPDAA PAGNGPTLRL ELEQEEEELE
DFLSPVRTPP GLVGAAAALQ PVPTKPLALQ NISLKHLGTE IQNTMYNIRS NRQAQGTGHG
PPGEDPPLSA EPQRAEWPLP SDPGTPGKDP ADSPKPTPKS SLTANLIQKA KRPNNTFPLF
AEGLTRTRTA QEKILALEQQ VLMLTKELKS QKELVRILHK ALEAAQQEKR ASSAYLAAAE
DKDRLELVRH KVRQIAELGK RVEALERERE SLAQTAGLRE QQVQELQRHV QQLLEKNQAK
QQVICKLSEK VTWDFTHPPT QPPVPLGAAD RDFLSQQEKM EHLKDDMEAY RTQNRFLNSE
IHQVTKIWRR VAEKEKALLM KCAYLQAKNC QVESKYLAGL RRLQEAAGGE ATESSELLRQ
LTQEALQWEA GEASADGVEL SPISEYDEYG FLTVPNYEME DLKLLAKIQA LEVHSHHLLA
HEAVERPLRE RWAALGDLAP SVELKQLLRA GVPREHRPRV WKWLVQLRVR HLQSPGHYQE
LLSRGQVREH PAARQIELDL NRTFPNNKHF TCPTSTFPDK LRRVLLAFSW QNPTIGYCQG
LNRLAAIALL VLEEEESAFW CLVAIVETIM PADYYSKTLT SSQVDQRVLQ DLLLEKLPRL
MAHLGQYRVD LSFLTFNWFL VVFADSLISN ILLRVWDAFL YEGTKYNEEE ILRLQDSLEI
YQYLRFFTKT ICNSQKLMTI AFNDMNPFPM KQLRQLRRAH RERLEAELHE LEQLKAEYLE
TQSSRGPAVP DGCTSEDEGE GEA
