CING_DANRE
ID CING_DANRE Reviewed; 1161 AA.
AC Q1L8T5; A5D6T7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Cingulin {ECO:0000250|UniProtKB:Q9P2M7};
GN Name=cgn {ECO:0000250|UniProtKB:Q9P2M7}; ORFNames=si:dkey-204a24.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably plays a role in the formation and regulation of the
CC tight junction (TJ) paracellular permeability barrier. Note=Localizes
CC to the apical junction complex composed of tight and adherens
CC junctions. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9P2M7}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P59242}.
CC -!- SIMILARITY: Belongs to the cingulin family. {ECO:0000305}.
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DR EMBL; CR628394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139880; AAI39881.1; -; mRNA.
DR RefSeq; NP_001038227.1; NM_001044762.1.
DR AlphaFoldDB; Q1L8T5; -.
DR SMR; Q1L8T5; -.
DR STRING; 7955.ENSDARP00000102223; -.
DR PaxDb; Q1L8T5; -.
DR PRIDE; Q1L8T5; -.
DR GeneID; 100005752; -.
DR KEGG; dre:100005752; -.
DR CTD; 100005752; -.
DR ZFIN; ZDB-GENE-050208-72; cgnb.
DR eggNOG; ENOG502QPNG; Eukaryota.
DR InParanoid; Q1L8T5; -.
DR PhylomeDB; Q1L8T5; -.
DR Reactome; R-DRE-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR PRO; PR:Q1L8T5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR002928; Myosin_tail.
DR Pfam; PF01576; Myosin_tail_1; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Coiled coil; Reference proteome; Tight junction.
FT CHAIN 1..1161
FT /note="Cingulin"
FT /id="PRO_0000371433"
FT REGION 1..403
FT /note="Head"
FT /evidence="ECO:0000250"
FT REGION 29..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1161
FT /note="Tail"
FT /evidence="ECO:0000250"
FT REGION 1123..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..1128
FT /evidence="ECO:0000255"
FT MOTIF 51..65
FT /note="ZIM"
FT COMPBIAS 82..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 62
FT /note="G -> S (in Ref. 2; AAI39881)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> ATSS (in Ref. 2; AAI39881)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="F -> S (in Ref. 2; AAI39881)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="T -> A (in Ref. 2; AAI39881)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118
FT /note="L -> LK (in Ref. 2; AAI39881)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1161 AA; 130821 MW; 91230C385436C4AB CRC64;
MSSLSADRKP PLDYGVQIRF IKDLDDAGGG FPDKSRLANG VGGVSNGTSS PSKYGVAVRV
QGISGQPYVV LQDGEKGDSY GVQLKTQPQI QSAPPVVSQT SPYNTLLLGQ REGARTPQGS
YNPTDQPSSP DEDFGSPLRR PPGDGQAGTQ GEAEPRTTER FTPSALAPKL DKKDNDAFNE
AGLRKVKQNG IGSSLNGTGL NGSFPPPSSA QDEDQAPAID TKSLAPINKL ISRFGGGGGG
SGDILNSEAQ TRPRLDNRVR SQSADALNKP SEEASSTSPT INPYAPNTSA TVPKLNSTKP
SSTGSLGRDA TSVAKVAAIP NFKPLAFNQS PKLFAPKEAP PAVPKKPVTP DLIKSQTTSI
ENGNGEDDQT KQAIYNILKE GSIEKEEAIK RKASLIHERF CGVKAPQISV TDSNMKTELE
QAFGRNTQLQ QQLDKSRREL QENQDQMVEL RMDREGAESR LRQQEDQLAQ LQEELRRTLE
NSPQSDSMQL DLLTVQAELS ESQLLRQKLE DTLRQREREL TALKGALKDE VASHDKEMEA
LREQFSQDMD ALRHSMETVS QSQLEIEEER QKVNASILAM EEELEGYKEQ SEQWKKQFSS
ANQELLKAQQ GKRELEEKLL AVVKQTDETD SNSVMKELQQ CRDSLKKAQS ELEKQKAETL
KKQEELKSAT RASEKRETEL KAEIDRLINQ LKKEKEELSK AIEKTQQPLV SDQTKDPESN
LELQEANARL RERIARMTRL HSSVPDSSSS DALEEENRSL KTQLEESRRA ASRLGVEKEE
LNRRLEERER EREALRRGKS DLEEQKRLLD RSLDKINKEM ESMMGDSRQS VQVLQSQLEE
FRDRSRRELQ DAQRLSKDRL VELQRAQALL KTTQEEVSRV KKELLSCTEE RDSTQLDKEL
LSSRLKNMET ELQTDRSSQT DRSREIRLLE DKVKTLEIEL DEEKSGAELL NERITRCREQ
VDQLRSELMQ ERSARHDLEM DKSALERQIK ELKSRIADMG TQSRPSAGVT MLENKVQELE
DRLRSEEREK NTIQAAQRRL DRKLKDVTAT LDQERNQHAE QRDQLSLRVK ALKRQLDESE
GEVERLEGVR RKVLRELEEQ RELQAALQAK VNAMDNELRK IQQSRRSTLG STLSSDEEDN
YSDTKSITSI LTDSPLQTTS C
