CING_CALJA
ID CING_CALJA Reviewed; 1204 AA.
AC B0KWC9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Cingulin {ECO:0000250|UniProtKB:Q9P2M7};
GN Name=CGN {ECO:0000250|UniProtKB:Q9P2M7};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (JAN-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}.
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DR EMBL; DP000572; ABY82100.1; -; Genomic_DNA.
DR AlphaFoldDB; B0KWC9; -.
DR STRING; 9483.ENSCJAP00000014335; -.
DR PRIDE; B0KWC9; -.
DR eggNOG; ENOG502R9EI; Eukaryota.
DR HOGENOM; CLU_002036_0_0_1; -.
DR InParanoid; B0KWC9; -.
DR Proteomes; UP000008225; Unplaced.
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;
KW Reference proteome; Tight junction.
FT CHAIN 1..1204
FT /note="Cingulin"
FT /id="PRO_0000371429"
FT REGION 7..359
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..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1204
FT /note="Tail"
FT /evidence="ECO:0000250"
FT COILED 360..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 169..187
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..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..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 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 581
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"
SQ SEQUENCE 1204 AA; 136814 MW; 7634D2F1C1FD7074 CRC64;
MEQAPNMAEP RGPVDHGVQI RFITEPVSGA EMGTLRRGGR RPAKDARAST YGVAVRVQGI
AGQPFVVLNS GEKGGDSFGV QIKGANDQGA SGALSSDSEL PENPYSQVRG FPAPSQSSTS
DEDPGTQWNG KLLRSQSQAS LAGPGPMDPS NRSTSMLDLA PKAASPGSTI DTAPLSSVDS
LINKFDSQLR GQARGRTGHR TRMLPPEQRK RSKSLDSRLP RDTLEERERQ STNHWNPNTK
YDNHVGSSKQ PAQSPSPSPS PLSGLSRARQ TQDWVLQSFE EPQGRAQDPT MLQFKSTPDL
LRDQQEAAPP GSVDHMKATI YGILREGSSE SETSVRRKVS LVLEKMQPLV MMSSGSSKAV
AGQGELTRKV EELQRKLDEE VKKRQKLEPS RVGLERQLEE KTEECSQLQE LLERRKGEAQ
QSNKELQNMK RLLDQGESLR HGLETQVVEL QNKLKQVQGP EPAKEVLLKD LLETRELLEE
VLEGKQRVEE QLRLRERELT ALKGALKEEV ASRDQEVEHV RQQCQRDTEQ LRKSMQDATQ
DHAVLEAERQ KMSALVRGLQ RELEETSEET GHWQSMFQKN KEELRATKQE LLQLRMEKEE
MEEELGEKIE VLQRELEQAR ASAGDTRQVE VLKKLCQTQE ELKELQAERQ SQEVAGRHRD
RELEKQLSVL RVEADRGREL EEQNFQLQKT LQQLRQNCEE ASKAKMVAEA EAAVLGQRRA
AVETTLRETQ EENDEFRRRI LGLEQQLKET RGLVDGGEAV EARLRDKLQR LEAEKQQLEE
ALNASQEEEG SLAAAKRALE ARLEEAQRGL ARLGQEQQTL NRALEEEGKQ REVLRRSKAE
LEEQKRLLDK TVDRLNKELE QIGEASKQAL QQLQSQLEDY KEKARREVAD AQRQAKDWAS
EAEKTSGGLN RLQDEIQRLR QALQACQAER DTAQLDKELL AQRLQGLEQE AENKKRSQDD
RARQLKGLEE KVSRLEAELD EEKNTVELLT DRVNRGRDQV DQLRTELMQE RSARQDLECD
KISLERQNKD LKTRLASSEG FQKPSASLSQ LESQNQLLQE RLQAEEREKT VLQSTNRKLE
RKVKELSIQI EDERQHVNDQ KDQLSLRVKA LKRQVDEAEE EIERLDGLRK KAQRELEEQH
EVNEQLQARI KSLEKDSWRK ASRSAAESTL KHEGLSSDEE FDGVYDPSSI ASLLTESNLQ
TSSC
