CING_CANLF
ID CING_CANLF Reviewed; 1196 AA.
AC A7YH32;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Cingulin {ECO:0000250|UniProtKB:Q9P2M7};
GN Name=CGN {ECO:0000250|UniProtKB:Q9P2M7};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=18097951; DOI=10.1080/09687680701474009;
RA Paschoud S., Citi S.;
RT "Inducible overexpression of cingulin in stably transfected MDCK cells does
RT not affect tight junction organization and gene expression.";
RL Mol. Membr. Biol. 25:1-13(2008).
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:0000250|UniProtKB:P59242}. Note=Localizes to the apical junction
CC complex composed of tight and adherens junctions. Colocalizes with
CC SPEF1 at sites of cell-cell contact in intestinal epithelial cells.
CC {ECO:0000250|UniProtKB:P59242, ECO:0000250|UniProtKB:Q9P2M7}.
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 -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI95366.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ910799; ABI95366.1; ALT_INIT; mRNA.
DR RefSeq; NP_001096687.1; NM_001103217.1.
DR AlphaFoldDB; A7YH32; -.
DR STRING; 9612.ENSCAFP00000018714; -.
DR PaxDb; A7YH32; -.
DR PRIDE; A7YH32; -.
DR Ensembl; ENSCAFT00845041833; ENSCAFP00845032813; ENSCAFG00845023683.
DR GeneID; 483198; -.
DR KEGG; cfa:483198; -.
DR CTD; 57530; -.
DR eggNOG; ENOG502R9EI; Eukaryota.
DR GeneTree; ENSGT00940000162698; -.
DR InParanoid; A7YH32; -.
DR Proteomes; UP000002254; Chromosome 17.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR InterPro; IPR002928; Myosin_tail.
DR Pfam; PF01576; Myosin_tail_1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell junction; Coiled coil; Phosphoprotein;
KW Reference proteome; Tight junction.
FT CHAIN 1..1196
FT /note="Cingulin"
FT /id="PRO_0000371428"
FT REGION 7..354
FT /note="Head"
FT /evidence="ECO:0000250"
FT REGION 54..67
FT /note="Interaction with TJP1/ZO1"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT REGION 82..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1196
FT /note="Tail"
FT /evidence="ECO:0000250"
FT COILED 355..1150
FT /evidence="ECO:0000255"
FT MOTIF 48..62
FT /note="ZIM"
FT COMPBIAS 82..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 576
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
SQ SEQUENCE 1196 AA; 136177 MW; AB7BC5D568534651 CRC64;
MEQASTMAEP RGPVDHGVQI RFITEPVGNA EMDTLRRGGR RPAKDARANT YGVAVRVQGI
AGQPFVVLNS GEQGSDSFGV QIKGTNNRGP PGALSSDSEL PESTYSHAKE FPARSQGSMS
DEELGAHWNG RLLRSQSQAS LKGPAPVSPS TRSTSLLQLA PEVASPGSTI DTAPLSSVDS
LINKFDSRQG GQARGRTGRR MRTLPPEQRK RSQSLDNRLP RDTLDEREHQ FPTHWTPSTK
RDSHMGNSKQ SSQNQGPLGG FSCSRQTQDW VLQSFEEPRG RAWDPGMLQF KSTPDLLRDQ
QETAPPGSVD HVKATIYSIL REGSSETETS VRRKVNLVLE QMQPLVMTSG SAKGLTGQSE
LSQKVEELQQ KLDEEVKKRP KLESSRLGLE RQLQEKAEEC SQLQELLERR KGEAQQSTKE
LQNMKLLVDQ SERVRCGLEA QVKELQDKLK QAQEPEPAKE ALMKDLLEAR ELLEEVLEGK
QRMEEHLRLR ERELTALKGA LKEEVASRDQ EVEHVRQQCQ RDAEQLRRSI QDATQDHAAL
EVERQKMSTL VRELQKELEE TSEETGHWQS MFQKNKDELR ATKQELLQLR MEKEEIEEEL
GEKIEVLQRE LGQARAGAAD TRQMEELKKE LCQTQKELKE LKEEQQNQEV AGRHRERELE
KQLKVEADRG QGLEQQNLQL QKTLQQLRQD CEEASKAQVA AEAEVAVLGQ RRAAVEVTLR
ETQEENDEFR RRILGLEQQL KEARGLAEGG EVAEARLRDK VQRLEAEKQR LEEALNAAQE
EEGSLAAAKR ALEARLEEAQ RGLARLGQEQ LALNRALEEE GKQREALRRS KAELEEQKRL
LDKTVCQLNK ELEQIGNDSK QALQQLQAQL EDYKEKARRE VADAQRQAKE WATEAEKNSG
GLSRLQDETQ RLRQALQASQ ADRDTARLDK ELLAQRLQGL EQEAENKKRS QDDRARQLKG
LEEKVSRLEA ELDEERSTVE LLTERVTRGR DQVDQLRSEL MQERSARQDL ECDKISLERQ
NKDLKSRLAS SEGFQKPSAS LSQLESQNQE LQERLQAEER EKTVLQSTNR KLERRVKELS
IQIDDERQHV NDQKDQLSLR VKALKRQVDE AEEEIERLDG LRKKAQRELE EQHEVNEQLQ
ARIKTLEKDS WRKASRSAAE SAQREGLSSD EEFDSVYDPS SIASLLTESN LQTSSC
