ID   TACD2_RAT               Reviewed;         317 AA.
AC   Q6P9Z6; Q6K0P4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Tumor-associated calcium signal transducer 2;
DE   AltName: Full=Parturition-related protein 1;
DE   Flags: Precursor;
GN   Name=Tacstd2; Synonyms=Prp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Huang Z., Myatt L., Ma R.Z.;
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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).
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   -!- SIMILARITY: Belongs to the EPCAM family. {ECO:0000305}.
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DR   EMBL; AY185508; AAO67351.1; -; mRNA.
DR   EMBL; BC060519; AAH60519.1; -; mRNA.
DR   RefSeq; NP_001009540.2; NM_001009540.2.
DR   AlphaFoldDB; Q6P9Z6; -.
DR   SMR; Q6P9Z6; -.
DR   STRING; 10116.ENSRNOP00000010156; -.
DR   GlyGen; Q6P9Z6; 4 sites.
DR   PaxDb; Q6P9Z6; -.
DR   PRIDE; Q6P9Z6; -.
DR   GeneID; 494343; -.
DR   KEGG; rno:494343; -.
DR   UCSC; RGD:1359498; rat.
DR   CTD; 4070; -.
DR   RGD; 1359498; Tacstd2.
DR   eggNOG; ENOG502QVSU; Eukaryota.
DR   InParanoid; Q6P9Z6; -.
DR   OrthoDB; 1017141at2759; -.
DR   PhylomeDB; Q6P9Z6; -.
DR   TreeFam; TF332767; -.
DR   PRO; PR:Q6P9Z6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0090191; P:negative regulation of branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR   GO; GO:2000146; P:negative regulation of cell motility; ISS:UniProtKB.
DR   GO; GO:0010633; P:negative regulation of epithelial cell migration; ISS:UniProtKB.
DR   GO; GO:1900028; P:negative regulation of ruffle assembly; ISS:UniProtKB.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; ISS:UniProtKB.
DR   GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR   GO; GO:2000738; P:positive regulation of stem cell differentiation; ISO:RGD.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:0060675; P:ureteric bud morphogenesis; ISO:RGD.
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   2: Evidence at transcript 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_0000380188"
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        37
FT                   /note="I -> V (in Ref. 1; AAO67351)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  35514 MW;  E5EF46E2DBA7143F CRC64;
     MARGLDLAPL LLLLLAMVAG FCTAQINCTC PTNKMTICNS NGPGGVCQCR AIGSQVLVDC
     STLTSKCLLL KARMSARKSS RRLVNPSEHA ILDNDGLYDP ECDDKGRFKA RQCNQTSVCW
     CVNSVGVRRT DKGDQSLRCD EVVRTHHILI ELRHRPTDRA FNHSDLDSEL RRLFKERYKL
     HPSFLAAVHY EEPTIQIELQ QNASQKGLRD VDIADAAYYF ERDIKGESLF VGRRGLDVQV
     RGEPLHVERT LIYYLDEKPP QFSMKRLTTG LIAVIAVVAV ALVAGVVVLV VTNRRKSGKY
     KKVELKELGE MRSEPSL