ID   CING_XENTR              Reviewed;        1259 AA.
AC   B1WB65;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Cingulin {ECO:0000250|UniProtKB:Q9P2M7};
GN   Name=cgn {ECO:0000250|UniProtKB:Q9P2M7};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-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, possibly by
CC       linking ZO proteins to the actomyosin cytoskeleton. {ECO:0000250}.
CC   -!- SUBUNIT: Parallel homodimer (By similarity). Interacts with TJP1/ZO1
CC       and TJP2/ZO2 (By similarity). {ECO:0000250|UniProtKB:Q9PTD7}.
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.
CC       {ECO:0000250|UniProtKB:P59242}.
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-9 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI61633.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC161633; AAI61633.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001120598.1; NM_001127126.1.
DR   AlphaFoldDB; B1WB65; -.
DR   STRING; 8364.ENSXETP00000044780; -.
DR   PaxDb; B1WB65; -.
DR   PRIDE; B1WB65; -.
DR   GeneID; 100145755; -.
DR   KEGG; xtr:100145755; -.
DR   CTD; 57530; -.
DR   Xenbase; XB-GENE-1009257; cgn.
DR   eggNOG; ENOG502R9EI; Eukaryota.
DR   InParanoid; B1WB65; -.
DR   OrthoDB; 110948at2759; -.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR   GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   InterPro; IPR002928; Myosin_tail.
DR   Pfam; PF01576; Myosin_tail_1; 2.
PE   2: Evidence at transcript level;
KW   Cell junction; Coiled coil; Reference proteome; Tight junction.
FT   CHAIN           1..1259
FT                   /note="Cingulin"
FT                   /id="PRO_0000371434"
FT   REGION          9..324
FT                   /note="Head"
FT                   /evidence="ECO:0000250"
FT   REGION          69..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          941..969
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1192..1259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1220..1259
FT                   /note="Tail"
FT                   /evidence="ECO:0000250"
FT   COILED          325..1218
FT                   /evidence="ECO:0000255"
FT   MOTIF           41..55
FT                   /note="ZIM"
FT   COMPBIAS        82..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1192..1231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1237..1259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1259 AA;  146939 MW;  07D6C5BFCAB36AFE CRC64;
     MERDLYGDMA DQPIPVGQGV QIRFINDLKE NGKPRGKRSK QDSYGVAVRV QGIDGQPFVV
     LNSGDKAKSS YDYDRHYSER SSTLDTAYSQ SSRESAWSRG SQKKTDNGEY PSLGYRSATS
     QQSTSASNKT NKNGLSTSSF SNQSSEDIDT KPLSSVDSLI TKFDVKGQVR GRTARRSQAL
     KDERKRSQSL DGRKNYQDTA DSREISLQQQ NEVPARRETV SSANRSFARQ SLEREDINKT
     RLTKEWLDQG GEEPVIVKQQ RSVQSEFQLK STPDLLRDQQ ADGSDPTREM IFSILRDGST
     ENENNLRKKT SILLEKFPSL QAQPGEDTRS LGSQKKELER KVAELQRQLD DEMKQRMKLE
     SSQGRPKAGM QRLEIQLEES KEECSRLKDL YDKKKNELNA VSQELMEVRM GKEQVETKLR
     AMEDKLMDSK EELSHLRAKG GTSPDKLALM KELEEVQDEL DEVLQIRQKQ EELLRQKDRE
     LTALKGALKD EVANHDKDLD RVREQYQNDV QQLRKNMENV SQDQLSLETE RQKINQVVRN
     LQRELEESSD EINQWKEMFQ KNKEELRSTK QELLQMKMEK EESEDELKET KDRFSLLQSE
     LEQAKKGSVD PGELASVRKE LQRVQDQLKQ LSVDKQKVEE NLHQRERELS ALKGALKEEV
     AGRGRETERL REQLQSEVVQ FKKDNENLGR ESQRIQDQLK QVLLEKQRHE EAVHQREREL
     SALKGALKDE VSGRDREAER LRAQFEQDAM QTKRSYEELV KINKRLESEK VDLERVRQVI
     ENNLQESREE NDDLRRKILG LEAQLKETNT FCDDLQRAES RLKDKITKLE TERKRMEDTL
     GEAADQEQEL AFVKRDLGNK LEEAQRSLKR LSLEYEELQE CYQEEMKQKD HLKKTKNELE
     EQKRLLDKSM DKLTRELDNM SNESRGSLQV LQSQLEEFRE KSRREIGEAQ KQAKEKTAEA
     ERHQFNSSRM QEEVQKLKLA LQELQVEKET VELDKQMVTQ RLQNLEQDTE SKKRVQDDRS
     RQVKVLEDKL KRMEAELDEE KNTVELLSDR INRSREQMEQ QRAELMQERA RGQDLECDKI
     SLERQNKDLK GRLANMEGQQ KPSVNVSHLE AKLQDIQERL QSEEREKATL LSTNRKLERK
     LKELNIQLED ERLHVNDQKD QLNLRVKALK RQVDEAEEEI ERLEGLRKKA VREMEEQQEL
     NEQLQTRLKT MEKESKRKPI RPAHNDDDDL SSDGEYGGSY DPSSITSLLT ESNLQTSSC