CLD2_HUMAN
ID CLD2_HUMAN Reviewed; 230 AA.
AC P57739; B2R6B9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Claudin-2;
DE AltName: Full=SP82;
GN Name=CLDN2; ORFNames=PSEC0059, SP82, UNQ705/PRO1356;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon epithelium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Skin;
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 [9]
RP SUMOYLATION AT LYS-218.
RX PubMed=22731716; DOI=10.1111/j.1749-6632.2012.06541.x;
RA Van Itallie C.M., Mitic L.L., Anderson J.M.;
RT "SUMOylation of claudin-2.";
RL Ann. N. Y. Acad. Sci. 1258:60-64(2012).
RN [10]
RP DISULFIDE BOND.
RX PubMed=23677799; DOI=10.1152/ajpcell.00074.2013;
RA Li J., Angelow S., Linge A., Zhuo M., Yu A.S.;
RT "Claudin-2 pore function requires an intramolecular disulfide bond between
RT two conserved extracellular cysteines.";
RL Am. J. Physiol. 305:C190-C196(2013).
RN [11]
RP INVOLVEMENT IN OAZON, AND VARIANT OAZON ARG-161.
RX PubMed=31320686; DOI=10.1038/s10038-019-0642-0;
RA Askari M., Karamzadeh R., Ansari-Pour N., Karimi-Jafari M.H., Almadani N.,
RA Sadighi Gilani M.A., Gourabi H., Vosough Taghi Dizaj A.,
RA Mohseni Meybodi A., Sadeghi M., Bashamboo A., McElreavey K., Totonchi M.;
RT "Identification of a missense variant in CLDN2 in obstructive
RT azoospermia.";
RL J. Hum. Genet. 64:1023-1032(2019).
CC -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC the intercellular space, through calcium-independent cell-adhesion
CC activity. {ECO:0000250|UniProtKB:O88552}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P57739; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-751440, EBI-10225815;
CC P57739; P78410: BTN3A2; NbExp=3; IntAct=EBI-751440, EBI-17564670;
CC P57739; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-751440, EBI-11749983;
CC P57739; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-751440, EBI-10267100;
CC P57739; Q07325: CXCL9; NbExp=3; IntAct=EBI-751440, EBI-3911467;
CC P57739; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-751440, EBI-3867333;
CC P57739; P54852: EMP3; NbExp=3; IntAct=EBI-751440, EBI-3907816;
CC P57739; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-751440, EBI-18304435;
CC P57739; Q14416: GRM2; NbExp=3; IntAct=EBI-751440, EBI-10232876;
CC P57739; P24593: IGFBP5; NbExp=3; IntAct=EBI-751440, EBI-720480;
CC P57739; Q6UWB1: IL27RA; NbExp=3; IntAct=EBI-751440, EBI-19045531;
CC P57739; Q15323: KRT31; NbExp=3; IntAct=EBI-751440, EBI-948001;
CC P57739; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-751440, EBI-11959885;
CC P57739; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-751440, EBI-11749135;
CC P57739; O43561-2: LAT; NbExp=3; IntAct=EBI-751440, EBI-8070286;
CC P57739; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-751440, EBI-12033434;
CC P57739; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-751440, EBI-945833;
CC P57739; P60201-2: PLP1; NbExp=3; IntAct=EBI-751440, EBI-12188331;
CC P57739; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-751440, EBI-10329860;
CC P57739; A2RU14: TMEM218; NbExp=3; IntAct=EBI-751440, EBI-10173151;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:O88552}. Cell membrane
CC {ECO:0000250|UniProtKB:O88552}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O88552}.
CC -!- PTM: The disulfide bond is necessary for pore formation, but is not
CC required for correct protein trafficking.
CC -!- DISEASE: Azoospermia, obstructive, with nephrolithiasis (OAZON)
CC [MIM:301060]: An X-linked recessive, male infertility disorder
CC characterized by epidydimal obstruction, hypercalciuria and kidney
CC stones. {ECO:0000269|PubMed:31320686}. Note=The disease may be caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AF250558; AAF98151.1; -; mRNA.
DR EMBL; AY358474; AAQ88838.1; -; mRNA.
DR EMBL; AK312515; BAG35416.1; -; mRNA.
DR EMBL; AF177340; AAG17984.1; -; mRNA.
DR EMBL; AK075371; BAC11575.1; -; mRNA.
DR EMBL; AK075405; BAG52130.1; -; mRNA.
DR EMBL; AL158821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471120; EAX02730.1; -; Genomic_DNA.
DR EMBL; CH471120; EAX02731.1; -; Genomic_DNA.
DR EMBL; BC014424; AAH14424.1; -; mRNA.
DR EMBL; BC071747; AAH71747.1; -; mRNA.
DR CCDS; CCDS14524.1; -.
DR RefSeq; NP_001164563.1; NM_001171092.1.
DR RefSeq; NP_001164566.1; NM_001171095.1.
DR RefSeq; NP_065117.1; NM_020384.3.
DR PDB; 4YYX; X-ray; 1.79 A; A/B=224-230.
DR PDBsum; 4YYX; -.
DR AlphaFoldDB; P57739; -.
DR SMR; P57739; -.
DR BioGRID; 114532; 28.
DR IntAct; P57739; 22.
DR STRING; 9606.ENSP00000441283; -.
DR iPTMnet; P57739; -.
DR PhosphoSitePlus; P57739; -.
DR BioMuta; CLDN2; -.
DR DMDM; 12229749; -.
DR jPOST; P57739; -.
DR MassIVE; P57739; -.
DR MaxQB; P57739; -.
DR PaxDb; P57739; -.
DR PeptideAtlas; P57739; -.
DR PRIDE; P57739; -.
DR ProteomicsDB; 57027; -.
DR Antibodypedia; 3617; 585 antibodies from 34 providers.
DR DNASU; 9075; -.
DR Ensembl; ENST00000336803.2; ENSP00000336571.1; ENSG00000165376.12.
DR Ensembl; ENST00000540876.1; ENSP00000443230.1; ENSG00000165376.12.
DR Ensembl; ENST00000541806.6; ENSP00000441283.1; ENSG00000165376.12.
DR GeneID; 9075; -.
DR KEGG; hsa:9075; -.
DR MANE-Select; ENST00000336803.2; ENSP00000336571.1; NM_020384.4; NP_065117.1.
DR UCSC; uc004emq.2; human.
DR CTD; 9075; -.
DR DisGeNET; 9075; -.
DR GeneCards; CLDN2; -.
DR GeneReviews; CLDN2; -.
DR HGNC; HGNC:2041; CLDN2.
DR HPA; ENSG00000165376; Tissue enhanced (choroid plexus, gallbladder, kidney, seminal vesicle).
DR MalaCards; CLDN2; -.
DR MIM; 300520; gene.
DR MIM; 301060; phenotype.
DR neXtProt; NX_P57739; -.
DR OpenTargets; ENSG00000165376; -.
DR PharmGKB; PA26567; -.
DR VEuPathDB; HostDB:ENSG00000165376; -.
DR eggNOG; ENOG502R10A; Eukaryota.
DR GeneTree; ENSGT00940000160785; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; P57739; -.
DR OMA; VWNIHVV; -.
DR OrthoDB; 1209440at2759; -.
DR PhylomeDB; P57739; -.
DR TreeFam; TF331936; -.
DR PathwayCommons; P57739; -.
DR Reactome; R-HSA-420029; Tight junction interactions.
DR SignaLink; P57739; -.
DR SIGNOR; P57739; -.
DR BioGRID-ORCS; 9075; 13 hits in 686 CRISPR screens.
DR ChiTaRS; CLDN2; human.
DR GeneWiki; CLDN2; -.
DR GenomeRNAi; 9075; -.
DR Pharos; P57739; Tbio.
DR PRO; PR:P57739; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P57739; protein.
DR Bgee; ENSG00000165376; Expressed in kidney epithelium and 90 other tissues.
DR Genevisible; P57739; HS.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISS: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; Disease variant;
KW Disulfide bond; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Tight junction; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..230
FT /note="Claudin-2"
FT /id="PRO_0000144734"
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:0000250|UniProtKB:O88552"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88552"
FT DISULFID 54..64
FT /evidence="ECO:0000269|PubMed:23677799"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:22731716"
FT VARIANT 161
FT /note="G -> R (in OAZON; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31320686"
FT /id="VAR_085653"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:4YYX"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:4YYX"
SQ SEQUENCE 230 AA; 24549 MW; 52CA642D4A62B70D CRC64;
MASLGLQLVG YILGLLGLLG TLVAMLLPSW KTSSYVGASI VTAVGFSKGL WMECATHSTG
ITQCDIYSTL LGLPADIQAA QAMMVTSSAI SSLACIISVV GMRCTVFCQE SRAKDRVAVA
GGVFFILGGL LGFIPVAWNL HGILRDFYSP LVPDSMKFEI GEALYLGIIS SLFSLIAGII
LCFSCSSQRN RSNYYDAYQA QPLATRSSPR PGQPPKVKSE FNSYSLTGYV
