TACD2_MOUSE
ID TACD2_MOUSE Reviewed; 317 AA.
AC Q8BGV3; O55130;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Tumor-associated calcium signal transducer 2;
DE AltName: Full=Cell surface glycoprotein Trop-2;
DE Flags: Precursor;
GN Name=Tacstd2; Synonyms=Trop2;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=9462726;
RX DOI=10.1002/(sici)1097-0215(19980119)75:2<324::aid-ijc24>3.0.co;2-b;
RA El Sewedy T., Fornaro M., Alberti S.;
RT "Cloning of the murine TROP2 gene: conservation of a PIP2-binding sequence
RT in the cytoplasmic domain of TROP-2.";
RL Int. J. Cancer 75:324-330(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Mammary gland, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: May function as a growth factor receptor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, lung, ovary and testis. High
CC levels of expression in immortalized keratinocytes.
CC {ECO:0000269|PubMed:9462726}.
CC -!- SIMILARITY: Belongs to the EPCAM family. {ECO:0000305}.
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DR EMBL; Y08830; CAA70063.1; -; Genomic_DNA.
DR EMBL; AK076410; BAC36328.1; -; mRNA.
DR EMBL; AK077370; BAC36773.1; -; mRNA.
DR EMBL; AK085753; BAC39531.1; -; mRNA.
DR EMBL; CH466523; EDK98807.1; -; Genomic_DNA.
DR EMBL; BC117719; AAI17720.1; -; mRNA.
DR EMBL; BC117720; AAI17721.1; -; mRNA.
DR CCDS; CCDS20221.1; -.
DR RefSeq; NP_064431.2; NM_020047.3.
DR AlphaFoldDB; Q8BGV3; -.
DR SMR; Q8BGV3; -.
DR STRING; 10090.ENSMUSP00000060099; -.
DR GlyGen; Q8BGV3; 4 sites.
DR iPTMnet; Q8BGV3; -.
DR PhosphoSitePlus; Q8BGV3; -.
DR MaxQB; Q8BGV3; -.
DR PaxDb; Q8BGV3; -.
DR PeptideAtlas; Q8BGV3; -.
DR PRIDE; Q8BGV3; -.
DR ProteomicsDB; 259340; -.
DR Antibodypedia; 33262; 649 antibodies from 45 providers.
DR DNASU; 56753; -.
DR Ensembl; ENSMUST00000058178; ENSMUSP00000060099; ENSMUSG00000051397.
DR GeneID; 56753; -.
DR KEGG; mmu:56753; -.
DR UCSC; uc009cfq.1; mouse.
DR CTD; 4070; -.
DR MGI; MGI:1861606; Tacstd2.
DR VEuPathDB; HostDB:ENSMUSG00000051397; -.
DR eggNOG; ENOG502QVSU; Eukaryota.
DR GeneTree; ENSGT00390000018245; -.
DR HOGENOM; CLU_075326_0_0_1; -.
DR InParanoid; Q8BGV3; -.
DR OMA; HYEHPTI; -.
DR OrthoDB; 1017141at2759; -.
DR PhylomeDB; Q8BGV3; -.
DR TreeFam; TF332767; -.
DR BioGRID-ORCS; 56753; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q8BGV3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BGV3; protein.
DR Bgee; ENSMUSG00000051397; Expressed in substantia propria of cornea and 104 other tissues.
DR Genevisible; Q8BGV3; MM.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0090191; P:negative regulation of branching involved in ureteric bud morphogenesis; IDA:UniProtKB.
DR GO; GO:2000146; P:negative regulation of cell motility; IDA:UniProtKB.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IDA:UniProtKB.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; IDA:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IDA:MGI.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IEP:UniProtKB.
DR GO; GO:0060675; P:ureteric bud morphogenesis; IEP:UniProtKB.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR043406; EPCAM/Trop-2.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR14168; PTHR14168; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF57610; SSF57610; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..317
FT /note="Tumor-associated calcium signal transducer 2"
FT /id="PRO_0000380187"
FT TOPO_DOM 25..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 64..139
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 113..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 121..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 187
FT /note="A -> V (in Ref. 1; CAA70063)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> V (in Ref. 1; CAA70063)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="L -> V (in Ref. 1; CAA70063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35574 MW; 6C54185B96A4C640 CRC64;
MARGLDLAPL LLLLLAMATR FCTAQSNCTC PTNKMTVCDT NGPGGVCQCR AMGSQVLVDC
STLTSKCLLL KARMSARKSG RSLVMPSEHA ILDNDGLYDP ECDDKGRFKA RQCNQTSVCW
CVNSVGVRRT DKGDQSLRCD EVVRTHHILI ELRHRPTDRA FNHSDLDSEL RRLFQERYKL
HPSFLSAVHY EEPTIQIELR QNASQKGLRD VDIADAAYYF ERDIKGESLF MGRRGLDVQV
RGEPLHVERT LIYYLDEKPP QFSMKRLTAG VIAVIAVVSV AVVAGVVVLV VTKRRKSGKY
KKVELKELGE MRSEPSL
