CING_PLEMO
ID CING_PLEMO Reviewed; 1204 AA.
AC B1MTG4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Cingulin {ECO:0000250|UniProtKB:Q9P2M7};
GN Name=CGN {ECO:0000250|UniProtKB:Q9P2M7};
OS Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC Pitheciidae; Callicebinae; Plecturocebus.
OX NCBI_TaxID=9523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (MAR-2008) 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. {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=ACA57938.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DP000634; ACA57938.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B1MTG4; -.
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 3: Inferred from homology;
KW Acetylation; Cell junction; Coiled coil; Phosphoprotein; Tight junction.
FT CHAIN 1..1204
FT /note="Cingulin"
FT /id="PRO_0000371430"
FT REGION 7..357
FT /note="Head"
FT /evidence="ECO:0000250"
FT REGION 25..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..67
FT /note="Interaction with TJP1/ZO1"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT REGION 68..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1204
FT /note="Tail"
FT /evidence="ECO:0000250"
FT COILED 358..1161
FT /evidence="ECO:0000255"
FT MOTIF 48..62
FT /note="ZIM"
FT COMPBIAS 88..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1179
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 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 579
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
SQ SEQUENCE 1204 AA; 136244 MW; 40A462738AD016C5 CRC64;
MEQAPNMAEP RGPVDHGVQI RFITEPVSGA EMGTLRRGGR RPAKDARAST YGVAVRVQGI
AGQPFVVLNS GEKGGDSFGV QIKGASDQGA SGALSSDSEL PENPYSQVQG FPAPSQSSTS
DEDPGAQWNG KLLRSQSQAS LAGPGPVDPS NRSTSMLDLA PKVASPGSTI DTAPLSSVDS
LINKFDGQLG GQARGRTGRR TRMLPPEQRK RSKSLDSRLP RDTLEERERQ STNHWNPSTK
YNNHVGSLKQ PAQSPSPSPL SGFSRARQTQ DWVLQSFEEP RGRAQDPTML QFKSTPDLLR
DQQEAAPPGS VDHMKATIYG ILREGSSESE ASVRRKVSLV LEKMQPLGVI SSGSSKAMAG
QGELARKVEE LQRKLDDEVK KRQKLEPSRA GLERQLEEKT EECSQLQELL ERREGEAQQS
SKELQNMKRL LDQGESLQHG LETQVMELQS KLKQVQGPEP AKELLLKDLL ETRELLEEVL
EGKQRVEEQL RLRERELTAL KGALKEEVAS RDQEVEHVRQ QCQRDTEQLR KSMQDASQDH
AVLEAERQKM SALVRGLQRE LEETSEETGH WQSMFQKNKE ELRATKQELL QLRMEKEEME
EELGEKIEAL QRELEQARAS AGDARQVEVL KKELRRAQEE LEELQAERQS QEVAGRHRDR
ELEKQLAGLR VEADRGRELE EQNFQLQKTL QQLRHDCEEA SKARGMAAEA EATVLGQRRG
AVEAALRETQ GDNDELRRRV LGLEQQLRET RGLVDGGEAA EARLRDKLQR LEADKQRLEE
ALNASQEEEG SLAAAKRALE ARLEEAQRGL ARLGQEQQTL TRALEEEGKQ REALRRSKAE
LEEQKRLLDR TVDRLNEELE QIGEASKQAL QQLQAQLEEY KEKARREVAD AQRQAKDWAS
EAEKSSGGLN RLQDEIQRLR QALQACQAER DTAQLDKELL AQRLQGLEQE AENKKRSQDD
RARQLKGLEE KVSRLEAELD EEKNTVELLT DRVNRGRDQV DQLRTELMQE RSARQDLECD
KISLERQNKD LKTRLASSEG FQKPSASLSQ LESQNQLLQE RLQAEEREKT VLQSTNRKLE
RKVKELSIQI EDERQHVNDQ KDQLSLRVKA FFRQVDEAEE EIERLDSLRR KAQRELEEQH
EVNGQLQARV KSLEKDSWRK ASRSAAESAL KHEGLSSDEE FDSVYDPSSI ASLLTESNLQ
TSSC
