CING_XENLA
ID CING_XENLA Reviewed; 1368 AA.
AC Q9PTD7; Q5BJ25;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cingulin {ECO:0000250|UniProtKB:Q9P2M7};
GN Name=cgn {ECO:0000250|UniProtKB:Q9P2M7};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, AND INTERACTION WITH TJP1;
RP TJP2; TJP3 AND MYOSIN.
RC TISSUE=Oocyte;
RX PubMed=10613913; DOI=10.1083/jcb.147.7.1569;
RA Cordenonsi M., D'Atri F., Hammar E., Parry D.A.D., Kenrick-Jones J.,
RA Shore D., Citi S.;
RT "Cingulin contains globular and coiled-coil domains and interacts with ZO-
RT 1, ZO-2, ZO-3 and myosin.";
RL J. Cell Biol. 147:1569-1582(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION IN TIGHT JUNCTION BIOGENESIS.
RX PubMed=8875080;
RX DOI=10.1002/(sici)1097-0177(199609)207:1<104::aid-aja10>3.0.co;2-0;
RA Cardellini P., Davanzo G., Citi S.;
RT "Tight junctions in early amphibian development: detection of junctional
RT cingulin from the 2-cell stage and its localization at the boundary of
RT distinct membrane domains in dividing blastomeres in low calcium.";
RL Dev. Dyn. 207:104-113(1996).
RN [4]
RP FUNCTION IN TIGHT JUNCTION BIOGENESIS.
RX PubMed=10940624; DOI=10.1016/s0925-4773(00)00368-3;
RA Fesenko I., Kurth T., Sheth B., Fleming T.P., Citi S., Hausen P.;
RT "Tight junction biogenesis in the early Xenopus embryo.";
RL Mech. Dev. 96:51-65(2000).
RN [5]
RP INTERACTION WITH OCLN.
RX PubMed=10491082; DOI=10.1046/j.1432-1327.1999.00616.x;
RA Cordenonsi M., Turco F., D'Atri F., Hammar E., Martinucci G., Meggio F.,
RA Citi S.;
RT "Xenopus laevis occludin. Identification of in vitro phosphorylation sites
RT by protein kinase CK2 and association with cingulin.";
RL Eur. J. Biochem. 264:374-384(1999).
RN [6]
RP INTERACTION WITH F-ACTIN.
RX PubMed=11682052; DOI=10.1016/s0014-5793(01)02936-2;
RA D'Atri F., Citi S.;
RT "Cingulin interacts with F-actin in vitro.";
RL FEBS Lett. 507:21-24(2001).
RN [7]
RP INTERACTION WITH TJP1.
RX PubMed=12023291; DOI=10.1074/jbc.m203717200;
RA D'Atri F., Nadalutti F., Citi S.;
RT "Evidence for a functional interaction between cingulin and ZO-1 in
RT cultured cells.";
RL J. Biol. Chem. 277:27757-27764(2002).
CC -!- FUNCTION: Probably plays a role in the formation and regulation of the
CC tight junction (TJ) paracellular permeability barrier, possibly by
CC linking ZO proteins to the actomyosin cytoskeleton.
CC {ECO:0000269|PubMed:10940624, ECO:0000269|PubMed:8875080}.
CC -!- SUBUNIT: Parallel homodimer (PubMed:10613913). Interacts with TJP1/ZO1
CC and TJP2/ZO2 in vivo, and TJP3/ZO3, myosin and OCLN in vitro, possibly
CC directly (PubMed:10613913, PubMed:10491082, PubMed:12023291). Acts as
CC an F-actin bundling protein in vitro (PubMed:11682052).
CC {ECO:0000269|PubMed:10491082, ECO:0000269|PubMed:10613913,
CC ECO:0000269|PubMed:12023291}.
CC -!- INTERACTION:
CC Q9PTD7; Q9PUN1: ocln; NbExp=2; IntAct=EBI-79525, EBI-79607;
CC Q9PTD7; Q91049: OCLN; Xeno; NbExp=2; IntAct=EBI-79525, EBI-79619;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P59242}. Note=Localizes to the apical junction
CC complex composed of tight and adherens junctions.
CC {ECO:0000250|UniProtKB:P59242}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9PTD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9PTD7-2; Sequence=VSP_037042;
CC -!- TISSUE SPECIFICITY: Localized on the cytoplasmic face of tight
CC junctions of polarized epithelia and some endothelia.
CC -!- DEVELOPMENTAL STAGE: A maternally synthesized protein. Found in the
CC apical cortex in the fertilized egg, where it is associated with
CC cytoskeleton filaments, it is recruited to tight junctions before
CC TJP1/ZO1 and OCLN. Nascent tight junctions are in place by the two-cell
CC stage.
CC -!- DOMAIN: Deletion of the TJP1/ZO1 interaction motif (ZIM) decreases but
CC does not abolish colocalization with TJP1/ZO1.
CC -!- SIMILARITY: Belongs to the cingulin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH91650.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF207901; AAF20208.1; -; mRNA.
DR EMBL; BC091650; AAH91650.1; ALT_INIT; mRNA.
DR RefSeq; NP_001081970.1; NM_001088501.1.
DR AlphaFoldDB; Q9PTD7; -.
DR BioGRID; 99484; 5.
DR IntAct; Q9PTD7; 5.
DR MINT; Q9PTD7; -.
DR PRIDE; Q9PTD7; -.
DR GeneID; 398149; -.
DR KEGG; xla:398149; -.
DR CTD; 398149; -.
DR Xenbase; XB-GENE-1009260; cgn.L.
DR Proteomes; UP000186698; Chromosome 8L.
DR GO; GO:0005923; C:bicellular tight junction; NAS:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR InterPro; IPR002928; Myosin_tail.
DR Pfam; PF01576; Myosin_tail_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Coiled coil; Reference proteome;
KW Tight junction.
FT CHAIN 1..1368
FT /note="Cingulin"
FT /id="PRO_0000089765"
FT REGION 9..435
FT /note="Head"
FT REGION 9..378
FT /note="Interaction with TJP3/ZO3 and myosin"
FT REGION 71..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..294
FT /note="Interaction with F-actin"
FT REGION 150..295
FT /note="Interaction with TJP2/ZO2"
FT REGION 278..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..1368
FT /note="Interaction with myosin"
FT REGION 1053..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1368
FT /note="Tail"
FT COILED 436..1330
FT /evidence="ECO:0000255"
FT MOTIF 41..55
FT /note="ZIM"
FT COMPBIAS 71..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 563..633
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_037042"
FT CONFLICT 395
FT /note="S -> N (in Ref. 2; AAH91650)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="H -> Q (in Ref. 2; AAH91650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1368 AA; 159446 MW; DB6D493B06DF1E42 CRC64;
MERDIYGDMA DQHIPVGQGV QIRFIGDLKE NGKPRGKRSK QDSYGVAVRV QGIDGQPFVV
LNSGDKAKSS FGVQIKSQEP YLNASNTSPP NYQNYSSKPR GPSRSISSES ELPENPYGSR
GYRPSSSHYS SASDEEQKPR GNIRGSDGLS SLPRPLQASR REELRRSQSH SSLLEPDVEE
SYDYDHHYSE RSSTLDTTYS QSSRDSAWSR SSQKKIDNGD YPSLGYRSAT SQQSTSVSNK
TKKNGLSTSS PSNQSNEDID TKPLSSVDSL INKFDIKGQV RGRTARRSQA LKDERKRSQS
LDGRKNYHDT ADSREIIVEK QNEVQTMREP VNASNRSFNR QTLERGDISK TRLTKEWLDQ
DREEPVILKQ QRTVQSEFQL KSTPDLLRDQ QPDGSDPTRE MIFGILREGS LESENTLRKK
TSILLEKLPS LQVQPGEDTI SLGSQKKELE RKVAELQRQL DDEMKQRMKL ETSQGRPKAG
MQRLEIELEE SKEECSRLKE LYEKKKNELS AMSQELMEVR MGKEQVETKL RTMEDKLMDS
KEELSHLRAK GGTSPDKLAL LKELEEVQDE LDEVLQIRQK QEELLRQKDR ELTALKGALK
DEVANHDKDL DRVREQYQND MQQLRKNMDN VSQDQLSLES ERQKINQVVR NLQRELEESS
DEISQWKEMF QKNKEELRST KQELLQMKLE KEESEDELKE TRDRFSLLQS ELAQVKKGSV
DPGEVASVRK ELQRVQDQLK QLSVDKQKVE ENLQQREREM SALKGTLKEE VSGRDRETVR
LREQLQSEVM HVKKENEGLA KESRRIQDQL KQVLLEKQRH EETVHQRERE LSVLKGALKD
EVSGRDRETE KLRERLEQDA LMTKRSYEEL VKINKRLESE KTDLERVRQV IENNLQESRE
ENDDLRRKIL GLEAQLKETN TFCDDLQRAE SRLKDKINKL EAERKRMEDS LGEVADQEQE
LAFVKRDLES KLDEAQRSLK RLSLEYEELQ ECYQEEMKQK DHLKKTKNEL EEQKRLLDKS
MDKLTRELDN MSNESRGSLQ LLQTQLEEYR EKSRKEIGEA QKQAKEKTAE AERHQFNSSR
MQEEVQKLKL ALQELQVEKE TVELDKQMIS QRLQSLEQDI ESKKRVQDDR SRQVKVLEDK
LKRMEAELDE EKNTVELLTD RVNRSRDQME QQRAELNQER SRGQDLECDK ISLERQNKEL
KNRLASMEGQ QKPSVNVSHL EAKLQEIQER LQLEEREKAT LLSTNRKLER KLKELNIQLE
DERLQVNDQK DQLNLRVKAL KRQVDEAEEE IERLEGLRKK AVREMEEQQE INEQLQTRVK
VMEKESKRKP IRPAHDDDLS SDGEFGGPYD PSSITSLLTE SNLQTSSC
