CING_MOUSE
ID CING_MOUSE Reviewed; 1191 AA.
AC P59242; Q05BC4; Q69ZM0; Q6P2K0;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Cingulin {ECO:0000305};
GN Name=Cgn {ECO:0000312|MGI:MGI:1927237}; Synonyms=Kiaa1319;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Trophoblast stem cell;
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 [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15292197; DOI=10.1074/jbc.m402616200;
RA Ohnishi H., Nakahara T., Furuse K., Sasaki H., Tsukita S., Furuse M.;
RT "JACOP, a novel plaque protein localizing at the apical junctional complex
RT with sequence similarity to cingulin.";
RL J. Biol. Chem. 279:46014-46022(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-92; SER-134 AND
RP SER-326, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-89; SER-90; SER-129;
RP SER-131; SER-134; SER-326; SER-339 AND SER-448, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Testis;
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).
CC -!- FUNCTION: Probably plays a role in the formation and regulation of the
CC tight junction (TJ) paracellular permeability barrier. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with TJP1/ZO1 and SPEF1
CC (By similarity). {ECO:0000250|UniProtKB:Q9P2M7}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:15292197}. Note=Localizes to the apical junction
CC complex composed of tight and adherens junction (PubMed:15292197).
CC Colocalizes with SPEF1 at sites of cell-cell contact in intestinal
CC epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q9P2M7,
CC ECO:0000269|PubMed:15292197}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P59242-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P59242-2; Sequence=VSP_037041;
CC -!- TISSUE SPECIFICITY: Lung, kidney and intestine.
CC {ECO:0000269|PubMed:15292197}.
CC -!- DOMAIN: Deletion of the TJP1/ZO1 interaction motif (ZIM) decreases but
CC does not abolish colocalization with TJP1/ZO1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cingulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42459.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH52941.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH52941.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH64474.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32426.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173148; BAD32426.1; ALT_INIT; mRNA.
DR EMBL; BC042459; AAH42459.1; ALT_INIT; mRNA.
DR EMBL; BC052941; AAH52941.1; ALT_SEQ; mRNA.
DR EMBL; BC064474; AAH64474.1; ALT_INIT; mRNA.
DR CCDS; CCDS50984.2; -. [P59242-1]
DR CCDS; CCDS79976.2; -. [P59242-2]
DR AlphaFoldDB; P59242; -.
DR SMR; P59242; -.
DR STRING; 10090.ENSMUSP00000102894; -.
DR iPTMnet; P59242; -.
DR PhosphoSitePlus; P59242; -.
DR MaxQB; P59242; -.
DR PaxDb; P59242; -.
DR PeptideAtlas; P59242; -.
DR PRIDE; P59242; -.
DR ProteomicsDB; 281624; -. [P59242-1]
DR ProteomicsDB; 281625; -. [P59242-2]
DR MGI; MGI:1927237; Cgn.
DR eggNOG; ENOG502R9EI; Eukaryota.
DR InParanoid; P59242; -.
DR PhylomeDB; P59242; -.
DR Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR ChiTaRS; Cgn; mouse.
DR PRO; PR:P59242; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P59242; protein.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:MGI.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR InterPro; IPR002928; Myosin_tail.
DR Pfam; PF01576; Myosin_tail_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell junction; Coiled coil;
KW Phosphoprotein; Reference proteome; Tight junction.
FT CHAIN 1..1191
FT /note="Cingulin"
FT /id="PRO_0000089764"
FT REGION 1..345
FT /note="Head"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..61
FT /note="Interaction with TJP1/ZO1"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT REGION 63..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1191
FT /note="Tail"
FT COILED 343..1150
FT /evidence="ECO:0000255"
FT MOTIF 42..56
FT /note="ZIM"
FT COMPBIAS 68..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 567
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT VAR_SEQ 337..344
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037041"
FT CONFLICT 430
FT /note="E -> K (in Ref. 2; AAH52941)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="K -> M (in Ref. 2; AAH52941)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="T -> A (in Ref. 2; AAH52941)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="R -> Q (in Ref. 1; BAD32426)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="M -> V (in Ref. 1; BAD32426)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="Q -> R (in Ref. 1; BAD32426)"
FT /evidence="ECO:0000305"
FT CONFLICT 1173
FT /note="D -> N (in Ref. 2; AAH52941/AAH64474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1191 AA; 136447 MW; 43EA20F49AF5E7D9 CRC64;
MADPRGPVDH GVQIRFITEP EGATEMGTLR RSGRRPARDA RASTYGVAVR VQGIAGQPFV
VLNSGEKGTD SFGVQIKGGN NRGSPGALSS DSELPENPYS QVKGRPATSR SSTSDEEPKD
HLNGKLIRSQ SQASLTGLAF MSPSNRSTSL LELAPKPTSS INTIDTAPLS SVDSLINKFD
SQKGGQVRGR TGRRTRTLPH EQRKRSQSLD SRLPRDTREE REHQSANHWT RGTKYDNHVD
SSKNPSQKQS PFSSFSRSRQ TQDWVLQSFE ETRDPAMVQF KSTPDLLRDQ RETAPPGSAD
HVKATIYGIL REGSSESEAS VRRKVSLVLE QMQPLGMVSP ASTKALAGQA ELTRKMEELQ
KKLDEEVKKR QKLEPSRVGL ERQLEEKAEE CHRLQELLER RKGEVQQSSK ELQNMKLLLG
QEEGLRHGLE AQVKELQLKL KHSQSPDSGK ESLLKDLLDT RELLEELLEG KQRVEEQLRL
RERELTALKG ALKEEVASHD QEVEHVRLQY QRDTEQLRRS MQDATQDHAA LEAERQKMSS
LVRELQRELE ETSEETGHWQ SMFQKNKEEL RATKQELLQL RMEKEEMEEE LGEKMEVLQR
DLEQARASTR DTHQVEELKK ELRRTQGELK ELQAEQQNQE VTGRHRNQVL EKQLAALREE
ADRGRELEQQ NLQLQKTLQQ LRQDCEEASK AKVASETEAM MLGQRRATVE TTLRETQEEN
DEFRRRILGL EQQLKEARGL AEGGEAVEAR LRDKVHRLEV EKQQLEEALN AAQEEEGNLA
AAKRALEVRL DEAQRGLARL GQEQQALNRA LEEEGKQREA LRRSKAELEE QKRLLNRTVD
RLNKELEQIG DDSKLALQQL QAQMEDYKEK ARKEVADAQR QAKDWASEAE KNSGGLSRLQ
DELQRLRQAL QTSQAERDTA RLDKELLAQR LQGLEQEAEN KKRFQDDKAR QLKSLEEKVS
RLEAELDEEK NTVELLTDRV NRGRDQVDQL RTELMQERSA RQDLECDKIS LERQNKDLKT
RLASSEGFQK PSASLSQLES QNQLLQERLQ AEEREKTVLQ STNRKLERRV KELSIQIDDE
RQHVNDQKDQ LTLRVKALKR QVDEAEEEIE RLDSLRKKAQ RELEEQHEVN EQLQARIKSL
EKDAWRKASR SAAESALKQE GLSSDEEFDN VYDPSSIASL LTESNLQTSS C
