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CLD2_MOUSE
ID   CLD2_MOUSE              Reviewed;         230 AA.
AC   O88552;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Claudin-2;
GN   Name=Cldn2;
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 [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=9647647; DOI=10.1083/jcb.141.7.1539;
RA   Furuse M., Fujita K., Hiiragi T., Fujimoto K., Tsukita S.;
RT   "Claudin-1 and -2: novel integral membrane proteins localizing at tight
RT   junctions with no sequence similarity to occludin.";
RL   J. Cell Biol. 141:1539-1550(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
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 MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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   [4]
RP   FUNCTION.
RX   PubMed=10508613; DOI=10.1016/s0960-9822(99)80452-7;
RA   Kubota K., Furuse M., Sasaki H., Sonoda N., Fujita K., Nagafuchi A.,
RA   Tsukita S.;
RT   "Ca(2+)-independent cell-adhesion activity of claudins, a family of
RT   integral membrane proteins localized at tight junctions.";
RL   Curr. Biol. 9:1035-1038(1999).
RN   [5]
RP   INTERACTION WITH CLDN1 AND CLDN3.
RX   PubMed=10562289; DOI=10.1083/jcb.147.4.891;
RA   Furuse M., Sasaki H., Tsukita S.;
RT   "Manner of interaction of heterogeneous claudin species within and between
RT   tight junction strands.";
RL   J. Cell Biol. 147:891-903(1999).
RN   [6]
RP   INTERACTION WITH TJP1; TJP2 AND TJP3.
RX   PubMed=10601346; DOI=10.1083/jcb.147.6.1351;
RA   Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S.;
RT   "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and
RT   ZO-3, with the COOH termini of claudins.";
RL   J. Cell Biol. 147:1351-1363(1999).
RN   [7]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=11934881; DOI=10.1074/jbc.m110261200;
RA   Sakaguchi T., Gu X., Golden H.M., Suh E., Rhoads D.B., Reinecker H.-C.;
RT   "Cloning of the human claudin-2 5'-flanking region revealed a TATA-less
RT   promoter with conserved binding sites in mouse and human for caudal-related
RT   homeodomain proteins and hepatocyte nuclear factor-1alpha.";
RL   J. Biol. Chem. 277:21361-21370(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219 AND SER-223, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Liver;
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).
RN   [9]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=32149733; DOI=10.1172/jci127750;
RA   Curry J.N., Saurette M., Askari M., Pei L., Filla M.B., Beggs M.R.,
RA   Rowe P.S., Fields T., Sommer A.J., Tanikawa C., Kamatani Y., Evan A.P.,
RA   Totonchi M., Alexander R.T., Matsuda K., Yu A.S.;
RT   "Claudin-2 deficiency associates with hypercalciuria in mice and human
RT   kidney stone disease.";
RL   J. Clin. Invest. 130:1948-1960(2020).
CC   -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC       the intercellular space, through calcium-independent cell-adhesion
CC       activity. {ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:32149733}.
CC   -!- SUBUNIT: Can form homo- and heteropolymers with other CLDN.
CC       Homopolymers interact with CLDN3, but not CLDN1, homopolymers. Directly
CC       interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3.
CC       {ECO:0000269|PubMed:10562289, ECO:0000269|PubMed:10601346}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000269|PubMed:11934881, ECO:0000269|PubMed:32149733}. Cell
CC       membrane {ECO:0000269|PubMed:11934881}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11934881}.
CC   -!- TISSUE SPECIFICITY: Expressed in the kidney, liver and intestine, with
CC       higher levels in the ileum than in the jejunum. Low levels in the
CC       brain. {ECO:0000269|PubMed:11934881, ECO:0000269|PubMed:9647647}.
CC   -!- INDUCTION: By CDX1 and CDX2. Induction by CDX2, but not CDX1, is
CC       potentiated by TCF1. {ECO:0000269|PubMed:11934881}.
CC   -!- PTM: The disulfide bond is necessary for pore formation, but is not
CC       required for correct protein trafficking. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Both female and male Cldn2-knockout mice are
CC       similarly hypercalciuric compared to wild-type littermates. Cldn2-null
CC       mice are hypercalciuric due to a primary defect in renal tubule calcium
CC       transport and develop papillary nephrocalcinosis. Cldn2-null mice are
CC       also found to have increased net intestinal calcium absorption, but
CC       reduced paracellular calcium permeability in the colon, suggesting
CC       reduced intestinal calcium secretion. {ECO:0000269|PubMed:32149733}.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR   EMBL; AF072128; AAC27079.1; -; mRNA.
DR   EMBL; AK004990; BAB23725.1; -; mRNA.
DR   EMBL; BC015252; AAH15252.1; -; mRNA.
DR   EMBL; BC085494; AAH85494.1; -; mRNA.
DR   CCDS; CCDS30437.1; -.
DR   RefSeq; NP_057884.1; NM_016675.4.
DR   RefSeq; XP_006528553.1; XM_006528490.3.
DR   PDB; 4P5H; X-ray; 3.38 A; 1/2/3/4/P/Q/R/S/T/U/V/W/X/Y/Z=141-160.
DR   PDBsum; 4P5H; -.
DR   AlphaFoldDB; O88552; -.
DR   SMR; O88552; -.
DR   MINT; O88552; -.
DR   STRING; 10090.ENSMUSP00000054219; -.
DR   TCDB; 1.H.1.1.11; the claudin tight junction (claudin1) family.
DR   iPTMnet; O88552; -.
DR   PhosphoSitePlus; O88552; -.
DR   MaxQB; O88552; -.
DR   PaxDb; O88552; -.
DR   PeptideAtlas; O88552; -.
DR   PRIDE; O88552; -.
DR   ProteomicsDB; 285489; -.
DR   Antibodypedia; 3617; 585 antibodies from 34 providers.
DR   DNASU; 12738; -.
DR   Ensembl; ENSMUST00000054889; ENSMUSP00000054219; ENSMUSG00000047230.
DR   GeneID; 12738; -.
DR   KEGG; mmu:12738; -.
DR   UCSC; uc009ukl.2; mouse.
DR   CTD; 9075; -.
DR   MGI; MGI:1276110; Cldn2.
DR   VEuPathDB; HostDB:ENSMUSG00000047230; -.
DR   eggNOG; ENOG502R10A; Eukaryota.
DR   GeneTree; ENSGT00940000160785; -.
DR   HOGENOM; CLU_076370_1_2_1; -.
DR   InParanoid; O88552; -.
DR   OMA; VWNIHVV; -.
DR   OrthoDB; 1209440at2759; -.
DR   PhylomeDB; O88552; -.
DR   TreeFam; TF331936; -.
DR   BioGRID-ORCS; 12738; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Cldn2; mouse.
DR   PRO; PR:O88552; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; O88552; protein.
DR   Bgee; ENSMUSG00000047230; Expressed in choroid plexus epithelium and 116 other tissues.
DR   ExpressionAtlas; O88552; baseline and differential.
DR   Genevisible; O88552; MM.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR005411; Claudin2.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; PTHR12002; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01589; CLAUDIN2.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell junction; Cell membrane; Disulfide bond;
KW   Isopeptide bond; Membrane; Phosphoprotein; Reference proteome;
KW   Tight junction; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..230
FT                   /note="Claudin-2"
FT                   /id="PRO_0000144735"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..81
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..116
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..162
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          205..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..230
FT                   /note="Interactions with TJP1, TJP2 and TJP3"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   DISULFID        54..64
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        218
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:4P5H"
SQ   SEQUENCE   230 AA;  24484 MW;  38A7C074A1E0D5D2 CRC64;
     MASLGVQLVG YILGLLGLLG TSIAMLLPNW RTSSYVGASI VTAVGFSKGL WMECATHSTG
     ITQCDIYSTL LGLPADIQAA QAMMVTSSAM SSLACIISVV GMRCTVFCQD SRAKDRVAVV
     GGVFFILGGI LGFIPVAWNL HGILRDFYSP LVPDSMKFEI GEALYLGIIS ALFSLVAGVI
     LCFSCSPQGN RTNYYDGYQA QPLATRSSPR SAQQPKAKSE FNSYSLTGYV
 
 
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