CING_PAPAN
ID CING_PAPAN Reviewed; 1203 AA.
AC A9X1A5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Cingulin {ECO:0000250|UniProtKB:Q9P2M7};
GN Name=CGN {ECO:0000250|UniProtKB:Q9P2M7};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
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 (DEC-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. {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=ABY40800.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DP000542; ABY40800.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_001162426.1; NM_001168955.1.
DR AlphaFoldDB; A9X1A5; -.
DR STRING; 9555.ENSPANP00000011187; -.
DR GeneID; 100137421; -.
DR KEGG; panu:100137421; -.
DR CTD; 57530; -.
DR eggNOG; ENOG502R9EI; Eukaryota.
DR Proteomes; UP000028761; 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..1203
FT /note="Cingulin"
FT /id="PRO_0000371431"
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 89..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1203
FT /note="Tail"
FT /evidence="ECO:0000250"
FT COILED 358..1160
FT /evidence="ECO:0000255"
FT MOTIF 48..62
FT /note="ZIM"
FT COMPBIAS 109..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..195
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..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
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 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M7"
SQ SEQUENCE 1203 AA; 136918 MW; D47CFC8E104296AA CRC64;
MEQAPNMAEP RGPVDHGVQI RFITEPVSGA EMGTLRRGGR RPAKDARAST YGVAVRVQGI
AGQPFVVLNS GEKGGDSFGV QIKGANDQEA SGALGSDFEL PENPYSQVKG FPAPSQSSTS
DEEPGAYWNG KLLRSQSQAS LAGPGPMDPS NRSTSMLELA PKVASPGSTI DTAPLSSVDS
LINKFDSQLG GQSRGRTGRR TRMLPPEQRK RSKSLDSRLP RDTLEERERQ STNHWTPSTK
YDNHVGSSKQ PSQSQSPSPP SGFSRSRQTQ DWVLQSFEEP RGRAQDPTML QFKSTPDLLR
DQQEAAPPGS VDHMKATIYG ILREGSSESE TSVRRKVSLV LEKMQPLVMI SSGSTKAVAG
QGELTRKVEE LQRKLDEEVK RRQKLEPSRV GLERQLEEKT EECSRLQELL ERRKGEAQQS
NKELQNMKRL LDQGEGLRHG LEAQVMELQN KLKQVQGPEP AKEVLLKDLL ETRELLEEVL
EGKQRVEEQL RLRERELTAL KGALKEEVAS RDQEVEHVRQ QYQRDTEQLR RSMQDATQDH
AVLEAERQKM SALVRGLQRE LEETSEETGH WQSMFQKNKE DLRATKQELL QLRMEKEEME
EELGEKIEVL QRELEQARAS AGDTRQVEVL KKELLQTQEE LKELQAERQS QEVAGRHRDR
ELEKQLAVLR VEADRGRELE EQNLQLQKTL QQLRQDCEEA SKAKMVAEAE AAVLGQRRAA
VETTLRETQE ENDEFRRRIL GLEQQLKETR GLVDGGEAVE ARLRDKLQRL EAEKQQLEEA
LNASQEEEGS LAAAKRALEA RLEEAQRGLA RLGQEQQTLN RALEEEGKQR EVLRRGKAEL
EEQKHLLDRT VDRLNKELEK IGEDSKQALQ QLQAQLDDYK EKARREVADA QRQAKDWASE
AEKTSGGLSR LQDEIQRLRQ ALQASQAERD TARLDKELLA QRLQGLEQEA ENKKRSQDDR
ARQLKGLEEK VSRLEAELDE EKNTVELLTD RVNRGRDQVD QLRTELLQER SARQDLECDK
ISLERQNKDL KTRLASSEGF QKPSASLSQL ESQNQLLQER LQAEEREKTV LQSTNRKLER
KVKELSIQIE DERQHVNDQK DQLSLRVKAL KRQVDEAEEE IERLDGLRKK AQRELEEQHE
VNEQLQARIK SLEKDSWRKA SRSAAESALK HEGLSSDEEF DSVYDPSSIA SLLTESNLQT
SSC
