CING_SORAR
ID CING_SORAR Reviewed; 1153 AA.
AC B3EX63;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Cingulin {ECO:0000250|UniProtKB:Q9P2M7};
GN Name=CGN {ECO:0000250|UniProtKB:Q9P2M7};
OS Sorex araneus (Eurasian common shrew) (European shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX NCBI_TaxID=42254;
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 (JUN-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}.
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DR EMBL; DP000772; ACE75821.1; -; Genomic_DNA.
DR AlphaFoldDB; B3EX63; -.
DR SMR; B3EX63; -.
DR PRIDE; B3EX63; -.
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..1153
FT /note="Cingulin"
FT /id="PRO_0000371432"
FT REGION 1..342
FT /note="Head"
FT /evidence="ECO:0000250"
FT REGION 17..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..57
FT /note="Interaction with TJP1/ZO1"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1153
FT /note="Tail"
FT /evidence="ECO:0000250"
FT COILED 343..1110
FT /evidence="ECO:0000255"
FT MOTIF 38..52
FT /note="ZIM"
FT COMPBIAS 191..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 562
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
SQ SEQUENCE 1153 AA; 130489 MW; 1016BA2D69A7EA86 CRC64;
MAEPRGPVDH GVQIRFITEP AGDAQMRTGR RPAKDARANT YGVAVRVQGI AGQPFVVLNS
GEKGSESFGV QIKGAHRQGP PGAPHSDLEL PAEHSRPLAQ ENAGTWQGSV SDEELGDPWR
GRLLRSQSQA SLLGPAPLGP GHRSTSLLEL GPPGLGAGSA IDTAPLSSVD TLIHKFDRHQ
GGQARGRTGR RMRALPAEQR KRSQSLDSRH LRDPPEDRRS PIPWAPPSRP GSAGSSKQPA
PKPIPTSSYS RARQTQDWVL QNFEEPRTRA QDPAVLQFKS TPDLLRDQQE AAPPGSVEHV
KAALYGILRE GSSESDASVR RKVSLVLEQM QPLVMTTGSA KVLAGQGELA QKVEELQRKL
DEEVKKRQVL EPSRLELEQQ LEEKAEECLR LQELLERQKG ETRQSGTELQ NLRLLLDQAG
RVRSELETQV MELQDQLKQG PVPAKEGLMK DLLETRELLE EVLEGKQRVE EQLRQREREL
TALKGALKEE VASRDQEVEH VRQQCQRDTE QLRKSIQDAS QDQAALEAER QKMSALVRGL
QRELEETSEE TGHWQTMFQK NKEELRAAKQ ELLQLRMEKD EMEEELGEKM EALQRELGQA
RAGAGGSRQV EELRKLQGEA ERVRELEQQN LQLQKKTQQL SQDCAEATKA RGARMAAEAE
AALLVQRRTA VETTLQETQG ENDEFRRRIL GLEQQLKETR GLAEGGEAAE ARLRDKLQRL
EVEKQRLEEA LSEAQAEEGS LAAAKRALEA RLEEAQRGLS RMGQEQQALS RALEEEGKQR
EALRRGKAEL EEQKRLLDRT VERLNKELEQ IGEDSKQALH QLQSQLEDYK EKSRREVADA
QRQAKEWASE AEKSSGGLSR LQDETQRLRQ TLQASQADLD TARLDKELLA QRLQGLEQEA
EKKRRSQDDR TRQVKSLEEK VSRLEMELDE ERNTVELLTD RINRSRDQVD QLRTELMQER
SARQDLECDK ISLERQNKDL KGRLASLEGF QKPSASLSQL ESQNRELQER LQAEDREKTV
LQSTNRKLER RVKELSIQID DERQHVNDQK DQLSLKVKAL KRQVDEAEEE IERLDGLRKK
AQRELEEQHE ANEQLQARIR ALEKDSWRKA ARSAAESSLQ QEGLSSDEEF DGVYNPNSIA
SLLTESGLQT SSC
