ID   TBD2A_BOVIN             Reviewed;         925 AA.
AC   A6QP29;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=TBC1 domain family member 2A;
GN   Name=TBC1D2; Synonyms=TBC1D2A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC       protein(s). Signal effector acting as a linker between RAC1 and RAB7A,
CC       leading to RAB7A inactivation and further inhibition of cadherin
CC       degradation (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; BC149120; AAI49121.1; -; mRNA.
DR   RefSeq; NP_001095451.1; NM_001101981.1.
DR   AlphaFoldDB; A6QP29; -.
DR   SMR; A6QP29; -.
DR   STRING; 9913.ENSBTAP00000026052; -.
DR   PaxDb; A6QP29; -.
DR   PRIDE; A6QP29; -.
DR   Ensembl; ENSBTAT00000026052; ENSBTAP00000026052; ENSBTAG00000019550.
DR   GeneID; 513828; -.
DR   KEGG; bta:513828; -.
DR   CTD; 55357; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019550; -.
DR   VGNC; VGNC:35633; TBC1D2.
DR   eggNOG; KOG2058; Eukaryota.
DR   GeneTree; ENSGT00940000159937; -.
DR   HOGENOM; CLU_011278_0_0_1; -.
DR   InParanoid; A6QP29; -.
DR   OMA; KTICNSR; -.
DR   OrthoDB; 1162786at2759; -.
DR   TreeFam; TF317336; -.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000019550; Expressed in thyroid gland and 102 other tissues.
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; IEA:Ensembl.
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   Acetylation; Cell junction; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW   GTPase activation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..925
FT                   /note="TBC1 domain family member 2A"
FT                   /id="PRO_0000395193"
FT   DOMAIN          47..144
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          622..814
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..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..435
FT                   /note="Interaction with RAC1"
FT                   /evidence="ECO:0000250"
FT   REGION          904..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          302..475
FT                   /evidence="ECO:0000255"
FT   COILED          872..907
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYX2"
FT   MOD_RES         917
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYX2"
SQ   SEQUENCE   925 AA;  105045 MW;  EC8D16C7F0C09F2D CRC64;
     MEGAQESPAE SGSSVPWSEE PAGSAKVPEV SLSEESEGCT RPLEATPPKL CGYLSKFGGK
     GPIRGWKSRW FFFDERKCHL YYSRTAQDAN PLDSIDLSSA VFDCKADAEE GTFEIKTPNR
     IITLKAATKQ AMLYWLQQLQ MKRWEFHNSL PALPAAHDAA LAGNGPALRL ELEQEEEEEE
     AFLCPVKTPT DLVGVAAAWQ PVHARPLALQ NISLKHLGTE IQNTMCNIRG NKQTQGANHR
     PPGEDSPLIE ETQREEQPSP PGPGAPGKDP ANSLKSSLTT SLIRKAKSQS NTFPLFSEGL
     MRNRTAQEKV LALEQQVLML TKELKAQKEL VKILHKALEA AQQEKRVSSA YLAAAQDKDR
     LELVRHKVRQ IAELGRRVEA LERERESLAQ TASLQEQEIR ELQQHVQLLL DKNQAKQQVI
     CKLSEKVTQD FMKAPEEADR DFLSQQEKME HLKDDMEAYR TQNRFLNSEI HQVTKIWRKV
     AEKEKALLMK CAYLQAQNCQ VESKYLAGLR RLQEALGVEA GECSELLRQL IQEALQWEAS
     EASADSVVLS PSTISEYDEY GFLTVPNYEV EDLRLLAKIQ ALEVHSHHLL AHEAVERPLR
     ERWATLGELA PSAELKQLLR AGVPHEHRPR VWRWLIRLRV QHLQAPGCYQ ALLSRGQACK
     HSAARQIELD LNRTFPNNKH FTCPTSSFPD KLRRVLLAFS WQNPTIGYCQ GLNRLAAIAL
     LVLDEEESAF WCLVAIVETI MPADYYSKTL LASQVDQRVL QDLLLEKLPR LMAHLGQRHV
     DLSFITFNWF LVVFADSLIS NILLQVWDAF LYEGIKVVFR YALAIFKYNE EALLRLQDSL
     EIYQYLHFFT KTICDSRKLM HIAFNDMNPF PMKQLRQLRA AHRERLEAEL NELEQLKAEY
     LETRAAQGPA VPEGSPSEDE GEAEP