CGNL1_MOUSE
ID CGNL1_MOUSE Reviewed; 1298 AA.
AC Q6AW69; Q5U5U0; Q69ZB4; Q8BLZ5; Q8BZ26; Q9D2T3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Cingulin-like protein 1;
DE AltName: Full=Junction-associated coiled-coil protein;
GN Name=Cgnl1; Synonyms=Jacop, Kiaa1749;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-640 (ISOFORM 5), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1-641 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Testis, Vagina, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 804-1298 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-1298 (ISOFORM 3).
RC TISSUE=Embryonic intestine;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-298, AND
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-257; SER-284 AND
RP SER-679, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
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: May be involved in anchoring the apical junctional complex,
CC especially tight junctions, to actin-based cytoskeletons.
CC {ECO:0000269|PubMed:15292197}.
CC -!- SUBUNIT: Homodimer or oligomer (Probable). Interacts with CD2AP and
CC SH3BP1; probably part of a complex at cell junctions (By similarity).
CC {ECO:0000250|UniProtKB:Q0VF96, ECO:0000305|PubMed:15292197}.
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 junctions. In the liver and
CC kidney, it is also found along non-junctional actin filament bundles in
CC addition to the apical junction. {ECO:0000269|PubMed:15292197}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6AW69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AW69-2; Sequence=VSP_029947;
CC Name=3;
CC IsoId=Q6AW69-3; Sequence=VSP_029948, VSP_029950;
CC Name=4;
CC IsoId=Q6AW69-4; Sequence=VSP_029948;
CC Name=5;
CC IsoId=Q6AW69-5; Sequence=VSP_029948, VSP_029949;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the kidney
CC and lung. {ECO:0000269|PubMed:15292197}.
CC -!- DOMAIN: The head region is responsible for both junction and actin
CC filament-based distribution. {ECO:0000269|PubMed:15292197}.
CC -!- SIMILARITY: Belongs to the cingulin family. {ECO:0000305}.
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DR EMBL; AB186125; BAD34967.1; -; mRNA.
DR EMBL; AK018850; BAB31463.1; -; mRNA.
DR EMBL; AK036871; BAC29612.1; -; mRNA.
DR EMBL; AK040774; BAC30701.2; -; mRNA.
DR EMBL; BC031499; AAH31499.1; -; mRNA.
DR EMBL; BC039211; AAH39211.1; -; mRNA.
DR EMBL; AK173252; BAD32530.1; -; mRNA.
DR CCDS; CCDS23328.1; -. [Q6AW69-4]
DR RefSeq; NP_001291291.1; NM_001304362.1.
DR RefSeq; NP_080875.3; NM_026599.5.
DR AlphaFoldDB; Q6AW69; -.
DR SMR; Q6AW69; -.
DR BioGRID; 212704; 3.
DR STRING; 10090.ENSMUSP00000072672; -.
DR iPTMnet; Q6AW69; -.
DR PhosphoSitePlus; Q6AW69; -.
DR jPOST; Q6AW69; -.
DR MaxQB; Q6AW69; -.
DR PaxDb; Q6AW69; -.
DR PeptideAtlas; Q6AW69; -.
DR PRIDE; Q6AW69; -.
DR ProteomicsDB; 283895; -. [Q6AW69-1]
DR ProteomicsDB; 283896; -. [Q6AW69-2]
DR ProteomicsDB; 283897; -. [Q6AW69-3]
DR ProteomicsDB; 283898; -. [Q6AW69-4]
DR ProteomicsDB; 283899; -. [Q6AW69-5]
DR GeneID; 68178; -.
DR KEGG; mmu:68178; -.
DR UCSC; uc009qpb.2; mouse. [Q6AW69-2]
DR CTD; 84952; -.
DR MGI; MGI:1915428; Cgnl1.
DR eggNOG; ENOG502QSXG; Eukaryota.
DR InParanoid; Q6AW69; -.
DR OrthoDB; 110948at2759; -.
DR PhylomeDB; Q6AW69; -.
DR BioGRID-ORCS; 68178; 2 hits in 58 CRISPR screens.
DR ChiTaRS; Cgnl1; mouse.
DR PRO; PR:Q6AW69; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6AW69; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0150105; P:protein localization to cell-cell junction; ISO:MGI.
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; Phosphoprotein;
KW Reference proteome; Tight junction.
FT CHAIN 1..1298
FT /note="Cingulin-like protein 1"
FT /id="PRO_0000312876"
FT REGION 1..551
FT /note="Head"
FT REGION 161..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1298
FT /note="Tail"
FT COILED 605..1252
FT /evidence="ECO:0000255"
FT MOTIF 37..51
FT /note="ZIM"
FT /evidence="ECO:0000250"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VF96"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VF96"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VF96"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VF96"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VF96"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VF96"
FT VAR_SEQ 1..1184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029947"
FT VAR_SEQ 450
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029948"
FT VAR_SEQ 633..635
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029949"
FT VAR_SEQ 728..798
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_029950"
FT CONFLICT 464
FT /note="K -> I (in Ref. 2; BAC29612)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="S -> G (in Ref. 1; BAD34967)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="Q -> R (in Ref. 4; BAD32530)"
FT /evidence="ECO:0000305"
FT CONFLICT 948
FT /note="Q -> E (in Ref. 4; BAD32530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1298 AA; 148231 MW; 535EDD1B752B3752 CRC64;
MELYFGEYQH VQQEYGVHLR LASGDTPKPR NSQPSKAGSY GVSIRVQGID GHPYIVLNNT
ERCLAGTPFP ENAPSFPSSV INNLSLHPSN GTVLKENTPE ELQLPENPYL QTSPLRGQKQ
FSLHEGRNGV LERKDGPTKL PHVLNFQRHP ELLQPYDPEK NEVNAKKHHP PESPWLRNAT
EDGTNCKKSR NCFPKSYGSQ PNSPTSEDLA KTNMTAIRLC SSVVIEDPQK QTSVCVNVQR
CAKEGVGEET LSPRRKSPTA PSPQAYSETK KNRPDVLPFR RQDSAGPILD GARSRRSSSS
STTPTSATSL YKFLLDDQEC AIHADSVNRH ENRRYIPFLP GTGRDIDTCS IPGVDQLIEK
FDQKPGLQRR GRSGKRNRIN PDDRKRSRSV DSAFPFGLQG NTEYLTEFSR NLGKSSEHLL
RPSQVFPQRS VAQEHRGKHS PSSPPAKLQG GAQGAHPKPP LQNKDGKVLN KGRQESTGAC
APSLPAPNKK EEEIKIATAT LMLQNRAVAA TSDSGAKKIS VKTFPSDSST QATPDLLKGQ
QELTQQTNEE TAKQILYNYL KEGGTDNEDA TKRKVNLVFE KIQTLKSRAA GSAQGSNQAP
NSPSEGNSLL DQKNKLILEV SELQQQLQLE MKNQQNIKEE RERMREDLEE LRVRHQSQVE
ETATLQRRLE ESEGELRKSL EELFQVKMER EQHQTEIRDL QDQLSEMHDE LDSTKRSEDR
EKGALIEELL QAKQDLQDLL IAKEEQEDLL RKRERELTAL KGALKEEVSS HDQEMDKLKE
QYDAELQAFR ESVEEATKNV EVLASRSNSS EQSQAEADLR EKVLKEENEK LQGRIAELER
RAAQLQRQME DVKGDEAQAK ETLRKCESEV QQLEEALVHA RKEEKEATCA RRALEKELEQ
AQRELSQVSQ EQKELLEKLR DEAEQKEQLR KLKNEMESER WHLDKTIQKL QKEMADIAEA
SRTSSLELQK QLGEYKEKNR RELAEMQTQL KEKCLEVEKA RLAASKMQDE LRLKEEELQD
YQRAEEEALT KRQLLEQSLK DLEYELEAKS HLKDDRSRLI KQMEDKVSQL EIELEEERTN
ADLLSERITW SREQMEQMRS ELLQEKAAKQ DLECDKISLE RQNKDLKSRI IHLEGSYRSS
KEGLVVQMEA RIAELEDRLE NEERDRANLQ LSNRRLERKV KELVMQVDDE HLSLTDQKDQ
LSLRLKAMKR QVEEAEEEID RLESSKKKLQ RELEEQMGVN EQLQGQLNSL KKGLRLKTLS
SKVLDDSDDD DLSSDAGSLY EAPLSYAFPK DSTIASQI
