ID   CING_HUMAN              Reviewed;        1197 AA.
AC   Q9P2M7; Q5T386; Q9NR25;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JAN-2003, sequence version 2.
DT   22-JUL-2008, entry version 55.
DE   RecName: Full=Cingulin;
GN   Name=CGN; Synonyms=KIAA1319;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Neuroepithelium;
RX   MEDLINE=20499514; PubMed=11042084; DOI=10.1006/jsbi.2000.4284;
RA   Citi S., D'Atri F., Parry D.A.D.;
RT   "Human and Xenopus cingulin share a modular organization of the
RT   coiled-coil rod domain: predictions for intra- and intermolecular
RT   assembly.";
RL   J. Struct. Biol. 131:135-145(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20181126; PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI.
RT   The complete sequences of 150 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 368-376.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [5]
RP   INTERACTION WITH TJP1.
RX   MEDLINE=22140336; 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).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND MASS
RP   SPECTROMETRY.
RX   PubMed=16083285; DOI=10.1021/pr050048h;
RA   Kim J.-E., Tannenbaum S.R., White F.M.;
RT   "Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
RL   J. Proteome Res. 4:1339-1346(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
CC   -!- FUNCTION: Probably plays a role in the formation and regulation of
CC       the tight junction (TJ) paracellular permeability barrier.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with TJP1/ZO-1.
CC   -!- INTERACTION:
CC       Q07157:TJP1; NbExp=1; IntAct=EBI-79537, EBI-79553;
CC       P39447:Tjp1 (xeno); NbExp=1; IntAct=EBI-79537, EBI-79508;
CC       P31946:YWHAB; NbExp=1; IntAct=EBI-79537, EBI-359815;
CC       P61981:YWHAG; NbExp=1; IntAct=EBI-79537, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction (By
CC       similarity). Note=Localizes to the apical junction complex
CC       composed of tight and adherens junctions (By similarity).
CC   -!- TISSUE SPECIFICITY: Localized on the cytoplasmic face of tight
CC       junctions of polarized epithelia and some endothelia. Expressed in
CC       pancreas, kidney, liver and lung, but not in skeletal muscle,
CC       placenta, brain or heart.
CC   -!- DOMAIN: Deletion of the ZO-1 interaction motif (ZIM) decreases but
CC       does not abolish colocalization with ZO-1.
CC   -!- SIMILARITY: Belongs to the cingulin family.
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DR   EMBL; AF263462; AAF74498.1; ALT_INIT; mRNA.
DR   EMBL; AB037740; BAA92557.1; ALT_INIT; mRNA.
DR   EMBL; AL365436; CAI16590.1; ALT_INIT; Genomic_DNA.
DR   UniGene; Hs.591464; -.
DR   HSSP; O46345; 1L4A.
DR   IntAct; Q9P2M7; -.
DR   PhosphoSite; Q9P2M7; -.
DR   Ensembl; ENSG00000143375; Homo sapiens.
DR   KEGG; hsa:57530; -.
DR   H-InvDB; HIX0001061; -.
DR   HGNC; HGNC:17429; CGN.
DR   HPA; CAB017193; -.
DR   MIM; 609473; gene.
DR   PharmGKB; PA134938123; -.
DR   HOVERGEN; Q9P2M7; -.
DR   ArrayExpress; Q9P2M7; -.
DR   CleanEx; HS_CGN; -.
DR   GermOnline; ENSG00000143375; Homo sapiens.
DR   GO; GO:0005923; C:tight junction; NAS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   InterPro; IPR002928; Myosin_tail.
DR   Pfam; PF01576; Myosin_tail_1; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Coiled coil; Direct protein sequencing; Phosphoprotein;
KW   Tight junction.
FT   CHAIN         1   1197       Cingulin.
FT                                /FTId=PRO_0000089763.
FT   REGION        1    351       Head.
FT   REGION      106    400       Interacts with ZO-2.
FT   REGION     1155   1197       Tail.
FT   COILED      352   1154       Potential.
FT   MOTIF        42     56       ZIM.
FT   COMPBIAS    363    836       Glu-rich.
FT   MOD_RES     111    111       Phosphoserine (By similarity).
FT   MOD_RES     112    112       Phosphoserine (By similarity).
FT   MOD_RES     129    129       Phosphoserine (By similarity).
FT   MOD_RES     131    131       Phosphoserine.
FT   MOD_RES     134    134       Phosphoserine.
SQ   SEQUENCE   1197 AA;  136386 MW;  0C9375283ABAAF3D CRC64;
     MAEPRGPVDH GVQIRFITEP VSGAEMGTLR RGGRRPAKDA RASTYGVAVR VQGIAGQPFV
     VLNSGEKGGD SFGVQIKGAN DQGASGALSS DLELPENPYS QVKGFPAPSQ SSTSDEEPGA
     YWNGKLLRSH SQASLAGPGP VDPSNRSNSM LELAPKVASP GSTIDTAPLS SVDSLINKFD
     SQLGGQARGR TGRRTRMLPP EQRKRSKSLD SRLPRDTFEE RERQSTNHWT SSTKYDNHVG
     TSKQPAQSQN LSPLSGFSRS RQTQDWVLQS FEEPRRSAQD PTMLQFKSTP DLLRDQQEAA
     PPGSVDHMKA TIYGILREGS SESETSVRRK VSLVLEKMQP LVMVSSGSTK AVAGQGELTR
     KVEELQRKLD EEVKKRQKLE PSQVGLERQL EEKTEECSRL QELLERRKGE AQQSNKELQN
     MKRLLDQGED LRHGLETQVM ELQNKLKHVQ GPEPAKEVLL KDLLETRELL EEVLEGKQRV
     EEQLRLRERE LTALKGALKE EVASRDQEVE HVRQQYQRDT EQLRRSMQDA TQDHAVLEAE
     RQKMSALVRG LQRELEETSE ETGHWQSMFQ KNKEDLRATK QELLQLRMEK EEMEEELGEK
     IEVLQRELEQ ARASAGDTRQ VEVLKKELLR TQEELKELQA ERQSQEVAGR HRDRELEKQL
     AVLRVEADRG RELEEQNLQL QKTLQQLRQD CEEASKAKMV AEAEATVLGQ RRAAVETTLR
     ETQEENDEFR RRILGLEQQL KETRGLVDGG EAVEARLRDK LQRLEAEKQQ LEEALNASQE
     EEGSLAAAKR ALEARLEEAQ RGLARLGQEQ QTLNRALEEE GKQREVLRRG KAELEEQKRL
     LDRTVDRLNK ELEKIGEDSK QALQQLQAQL EDYKEKARRE VADAQRQAKD WASEAEKTSG
     GLSRLQDEIQ RLRQALQASQ AERDTARLDK ELLAQRLQGL EQEAENKKRS QDDRARQLKG
     LEEKVSRLET ELDEEKNTVE LLTDRVNRGR DQVDQLRTEL MQERSARQDL ECDKISLERQ
     NKDLKTRLAS SEGFQKPSAS LSQLESQNQL LQERLQAEER EKTVLQSTNR KLERKVKELS
     IQIEDERQHV NDQKDQLSLR VKALKRQVDE AEEEIERLDG LRKKAQREVE EQHEVNEQLQ
     ARIKSLEKDS WRKASRSAAE SALKNEGLSS DEEFDSVYDP SSIASLLTES NLQTSSC
//