TB10C_MOUSE
ID TB10C_MOUSE Reviewed; 444 AA.
AC Q8C9V1; Q3V3L7; Q6KAN0; Q8C2R6; Q8C6F7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Carabin;
DE AltName: Full=TBC1 domain family member 10C;
GN Name=Tbc1d10c;
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).
RC STRAIN=ICR; TISSUE=Spleen;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Pancreas, and 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inhibits the Ras signaling pathway through its intrinsic Ras
CC GTPase-activating protein (GAP) activity. Acts as a negative feedback
CC inhibitor of the calcineurin signaling pathway that also mediates
CC crosstalk between calcineurin and Ras (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with both calcineurin and HRAS. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8C9V1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C9V1-2; Sequence=VSP_024538;
CC Name=3;
CC IsoId=Q8C9V1-3; Sequence=VSP_024536;
CC Name=4;
CC IsoId=Q8C9V1-4; Sequence=VSP_024537, VSP_024539;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21427.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK131177; BAD21427.1; ALT_INIT; mRNA.
DR EMBL; AK038366; BAE20537.1; -; mRNA.
DR EMBL; AK040487; BAC30605.1; -; mRNA.
DR EMBL; AK075803; BAC35971.1; -; mRNA.
DR EMBL; AK088119; BAC40158.1; -; mRNA.
DR EMBL; AK146426; BAE27160.1; -; mRNA.
DR CCDS; CCDS37885.1; -. [Q8C9V1-1]
DR RefSeq; NP_848765.2; NM_178650.3. [Q8C9V1-1]
DR RefSeq; XP_006531689.1; XM_006531626.2. [Q8C9V1-1]
DR AlphaFoldDB; Q8C9V1; -.
DR SMR; Q8C9V1; -.
DR STRING; 10090.ENSMUSP00000042660; -.
DR iPTMnet; Q8C9V1; -.
DR PhosphoSitePlus; Q8C9V1; -.
DR EPD; Q8C9V1; -.
DR jPOST; Q8C9V1; -.
DR MaxQB; Q8C9V1; -.
DR PaxDb; Q8C9V1; -.
DR PRIDE; Q8C9V1; -.
DR ProteomicsDB; 262933; -. [Q8C9V1-1]
DR ProteomicsDB; 262934; -. [Q8C9V1-2]
DR ProteomicsDB; 262935; -. [Q8C9V1-3]
DR ProteomicsDB; 262936; -. [Q8C9V1-4]
DR Antibodypedia; 30378; 141 antibodies from 24 providers.
DR DNASU; 108995; -.
DR Ensembl; ENSMUST00000045864; ENSMUSP00000042660; ENSMUSG00000040247. [Q8C9V1-2]
DR Ensembl; ENSMUST00000235450; ENSMUSP00000158437; ENSMUSG00000040247. [Q8C9V1-1]
DR Ensembl; ENSMUST00000235487; ENSMUSP00000158162; ENSMUSG00000040247. [Q8C9V1-4]
DR Ensembl; ENSMUST00000236780; ENSMUSP00000158519; ENSMUSG00000040247. [Q8C9V1-4]
DR Ensembl; ENSMUST00000237495; ENSMUSP00000158341; ENSMUSG00000040247. [Q8C9V1-4]
DR GeneID; 108995; -.
DR KEGG; mmu:108995; -.
DR UCSC; uc008fze.1; mouse. [Q8C9V1-1]
DR UCSC; uc012bgh.1; mouse. [Q8C9V1-2]
DR CTD; 374403; -.
DR MGI; MGI:1922072; Tbc1d10c.
DR VEuPathDB; HostDB:ENSMUSG00000040247; -.
DR eggNOG; KOG2221; Eukaryota.
DR GeneTree; ENSGT00940000161287; -.
DR HOGENOM; CLU_005350_2_1_1; -.
DR InParanoid; Q8C9V1; -.
DR OMA; QRMACPG; -.
DR OrthoDB; 976276at2759; -.
DR PhylomeDB; Q8C9V1; -.
DR TreeFam; TF313293; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 108995; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Tbc1d10c; mouse.
DR PRO; PR:Q8C9V1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8C9V1; protein.
DR Bgee; ENSMUSG00000040247; Expressed in granulocyte and 57 other tissues.
DR ExpressionAtlas; Q8C9V1; baseline and differential.
DR Genevisible; Q8C9V1; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031527; C:filopodium membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0042113; P:B cell activation; IGI:MGI.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IMP:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0050869; P:negative regulation of B cell activation; IMP:MGI.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Reference proteome.
FT CHAIN 1..444
FT /note="Carabin"
FT /id="PRO_0000284468"
FT DOMAIN 90..278
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..444
FT /note="Interaction with calcineurin"
FT /evidence="ECO:0000250"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 135
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 176
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024536"
FT VAR_SEQ 155..180
FT /note="QQGLLQVLKAYTLYRPEQGYCQAQGP -> RGCCRFSRPTPCTGQSRDTARL
FT RDL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024537"
FT VAR_SEQ 181..444
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024539"
FT VAR_SEQ 215..231
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15449545"
FT /id="VSP_024538"
SQ SEQUENCE 444 AA; 49930 MW; C142EC1491874B7C CRC64;
MAQALGEDLL SELQDDSSSL GSDSELSGPS PYRQADRYGF IGGNSGELRL CQPSADLIRQ
REMKWVEMTL HWEKTMSRRY KKVKIQCRKG IPSALRARCW PLLCGARMCQ KNNPGTYQEL
AAAPGDPQWM ETIGRDLHRQ FPLHEMFVSP QGHGQQGLLQ VLKAYTLYRP EQGYCQAQGP
VAAVLLMHLP PEEAFWCLVQ ICEVYLPGYY GPHMEAVQLD AEVFMALLRR QLPRVYKHLQ
QVGVGPLLYL PEWFLCLFTR SLPFPTVLRI WDAFLSEGAK VLFRVGLTLM RLALGTVEQR
TACPGLLETL GALRAIPPTQ LQEEVFMSQV HSVTLSERVL QQEIRIQLAQ LSKSLPGPAP
LPQARLPGAQ AIFESQQLAG VRESTKPEIP RIVVQPPEEP KPPRRKPQTR GKTFHGLLIR
ARGPPIEGPS RSQRGSASFL DTRF
