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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Oocyte;
DOI=10.1083/jcb.147.7.1569; PubMed=10613913 [NCBI, ExPASy, EBI, Israel, Japan]
Cordenonsi M.,
D'Atri F.,
Hammar E.,
Parry D.A.D.,
Kenrick-Jones J.,
Shore D.,
Citi S.;
"Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2, ZO-3 and myosin.";
J. Cell Biol. 147:1569-1582(1999).
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[2]
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FUNCTION IN TIGHT JUNCTION BIOGENESIS.
DOI=10.1002/(SICI)1097-0177(199609)207:1<104::AID-AJA10>3.3.CO;2-D; PubMed=8875080 [NCBI, ExPASy, EBI, Israel, Japan]
Cardellini P.,
Davanzo G.,
Citi S.;
"Tight junctions in early amphibian development: detection of junctional cingulin from the 2-cell stage and its localization at the boundary of distinct membrane domains in dividing blastomeres in low calcium.";
Dev. Dyn. 207:104-113(1996).
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[3]
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FUNCTION IN TIGHT JUNCTION BIOGENESIS.
DOI=10.1016/S0925-4773(00)00368-3; PubMed=10940624 [NCBI, ExPASy, EBI, Israel, Japan]
Fesenko I.,
Kurth T.,
Sheth B.,
Fleming T.P.,
Citi S.,
Hausen P.;
"Tight junction biogenesis in the early Xenopus embryo.";
Mech. Dev. 96:51-65(2000).
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[4]
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INTERACTION WITH OCCLUDIN.
PubMed=10491082 [NCBI, ExPASy, EBI, Israel, Japan]
Cordenonsi M.,
Turco F.,
D'Atri F.,
Hammar E.,
Martinucci G.,
Meggio F.,
Citi S.;
"Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin.";
Eur. J. Biochem. 264:374-384(1999).
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[5]
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INTERACTION WITH F-ACTIN.
DOI=10.1016/S0014-5793(01)02936-2; PubMed=11682052 [NCBI, ExPASy, EBI, Israel, Japan]
D'Atri F.,
Citi S.;
"Cingulin interacts with F-actin in vitro.";
FEBS Lett. 507:21-24(2001).
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[6]
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INTERACTION WITH ZO-1.
DOI=10.1074/jbc.M203717200; PubMed=12023291 [NCBI, ExPASy, EBI, Israel, Japan]
D'Atri F.,
Nadalutti F.,
Citi S.;
"Evidence for a functional interaction between cingulin and ZO-1 in cultured cells.";
J. Biol. Chem. 277:27757-27764(2002).
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- FUNCTION: Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier, possibly by linking ZO proteins to the actomyosin cytoskeleton.
- SUBUNIT: Parallel homodimer (By similarity). Binds ZO-1 and ZO-2 in vivo, and ZO-3, myosin and occludin in vitro, possibly directly. Acts as an F-actin bundling protein in vitro.
- INTERACTION:
Self; NbExp=1; IntAct=EBI-79525, EBI-79525;
Q91049:OCLN (xeno); NbExp=2; IntAct=EBI-79525, EBI-79619;
Q9PUN1:ocln; NbExp=2; IntAct=EBI-79525, EBI-79607;
Q07157:TJP1 (xeno); NbExp=1; IntAct=EBI-79525, EBI-79553;
P39447:Tjp1 (xeno); NbExp=1; IntAct=EBI-79525, EBI-79508;
Q9Z0U1:Tjp2 (xeno); NbExp=1; IntAct=EBI-79525, EBI-79579;
- SUBCELLULAR LOCATION: Cell junction, tight junction (By similarity). Note=Localizes to the apical junction complex composed of tight and adherens junctions (By similarity).
- TISSUE SPECIFICITY: Localized on the cytoplasmic face of tight junctions of polarized epithelia and some endothelia.
- DEVELOPMENTAL STAGE: A maternally synthesized protein. Found in the apical cortex in the fertilized egg, where it is associated with cytoskeleton filaments, it is recruited to tight junctions before ZO-1 and occludin. Nascent tight junctions are in place by the two-cell stage.
- DOMAIN: Deletion of the ZO-1 interaction motif (ZIM) decreases but does not abolish colocalization with ZO-1.
- SIMILARITY: Belongs to the cingulin family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 1360 AA [This is the length of the unprocessed precursor] |
Molecular weight: 158466 Da [This is the MW of the unprocessed precursor] |
CRC64: 9D66CA572401B7B0 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MADQHIPVGQ GVQIRFIGDL KENGKPRGKR SKQDSYGVAV RVQGIDGQPF VVLNSGDKAK
70 80 90 100 110 120
SSFGVQIKSQ EPYLNASNTS PPNYQNYSSK PRGPSRSISS ESELPENPYG SRGYRPSSSH
130 140 150 160 170 180
YSSASDEEQK PRGNIRGSDG LSSLPRPLQA SRREELRRSQ SHSSLLEPDV EESYDYDHHY
190 200 210 220 230 240
SERSSTLDTT YSQSSRDSAW SRSSQKKIDN GDYPSLGYRS ATSQQSTSVS NKTKKNGLST
250 260 270 280 290 300
SSPSNQSNED IDTKPLSSVD SLINKFDIKG QVRGRTARRS QALKDERKRS QSLDGRKNYH
310 320 330 340 350 360
DTADSREIIV EKQNEVQTMR EPVNASNRSF NRQTLERGDI SKTRLTKEWL DQDREEPVIL
370 380 390 400 410 420
KQQRTVQSEF QLKSTPDLLR DQQPDGSDPT REMIFGILRE GSLESENTLR KKTSILLEKL
430 440 450 460 470 480
PSLQVQPGED TISLGSQKKE LERKVAELQR QLDDEMKQRM KLETSQGRPK AGMQRLEIEL
490 500 510 520 530 540
EESKEECSRL KELYEKKKNE LSAMSQELME VRMGKEQVET KLRTMEDKLM DSKEELSHLR
550 560 570 580 590 600
AKGGTSPDKL ALLKELEEVQ DELDEVLQIR QKQEELLRQK DRELTALKGA LKDEVANHDK
610 620 630 640 650 660
DLDRVREQYQ NDMQQLRKNM DNVSQDQLSL ESERQKINQV VRNLQRELEE SSDEISQWKE
670 680 690 700 710 720
MFQKNKEELR STKQELLQMK LEKEESEDEL KETRDRFSLL QSELAQVKKG SVDPGEVASV
730 740 750 760 770 780
RKELQRVQDQ LKQLSVDKQK VEENLQQRER EMSALKGTLK EEVSGRDRET VRLREQLQSE
790 800 810 820 830 840
VMHVKKENEG LAKESRRIQD QLKQVLLEKQ RHEETVHQRE RELSVLKGAL KDEVSGRDRE
850 860 870 880 890 900
TEKLRERLEQ DALMTKRSYE ELVKINKRLE SEKTDLERVR QVIENNLQES REENDDLRRK
910 920 930 940 950 960
ILGLEAQLKE TNTFCDDLQR AESRLKDKIN KLEAERKRME DSLGEVADQE QELAFVKRDL
970 980 990 1000 1010 1020
ESKLDEAQRS LKRLSLEYEE LQECYQEEMK QKDHLKKTKN ELEEQKRLLD KSMDKLTREL
1030 1040 1050 1060 1070 1080
DNMSNESRGS LQLLQTQLEE YREKSRKEIG EAQKQAKEKT AEAERHQFNS SRMQEEVQKL
1090 1100 1110 1120 1130 1140
KLALQELQVE KETVELDKQM ISQRLQSLEQ DIESKKRVQD DRSRQVKVLE DKLKRMEAEL
1150 1160 1170 1180 1190 1200
DEEKNTVELL TDRVNRSRDQ MEQQRAELNQ ERSRGQDLEC DKISLERQNK ELKNRLASME
1210 1220 1230 1240 1250 1260
GQQKPSVNVS HLEAKLQEIQ ERLQLEEREK ATLLSTNRKL ERKLKELNIQ LEDERLQVND
1270 1280 1290 1300 1310 1320
QKDQLNLRVK ALKRQVDEAE EEIERLEGLR KKAVREMEEQ QEINEQLQTR VKVMEKESKR
1330 1340 1350 1360
KPIRPAHDDD LSSDGEFGGP YDPSSITSLL TESNLQTSSC
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Q9PTD7 in FASTA format |
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