ID   CLD11_MACFA             Reviewed;         207 AA.
AC   Q4R3L1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Claudin-11;
GN   Name=CLDN11; ORFNames=QtsA-16119;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC       the intercellular space, through calcium-independent cell-adhesion
CC       activity. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with tetraspanin-3/TSPAN3. Interacts with OCLN.
CC       {ECO:0000250|UniProtKB:O75508, ECO:0000250|UniProtKB:Q60771}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Cell
CC       membrane {ECO:0000250|UniProtKB:O75508}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR   EMBL; AB179255; BAE02306.1; -; mRNA.
DR   RefSeq; NP_001271695.1; NM_001284766.1.
DR   AlphaFoldDB; Q4R3L1; -.
DR   SMR; Q4R3L1; -.
DR   STRING; 9541.XP_005546422.1; -.
DR   PRIDE; Q4R3L1; -.
DR   Ensembl; ENSMFAT00000017054; ENSMFAP00000042770; ENSMFAG00000040128.
DR   GeneID; 101925295; -.
DR   CTD; 5010; -.
DR   VEuPathDB; HostDB:ENSMFAG00000040128; -.
DR   eggNOG; ENOG502QSDJ; Eukaryota.
DR   GeneTree; ENSGT00890000139496; -.
DR   OMA; AHRETMI; -.
DR   OrthoDB; 1223820at2759; -.
DR   Proteomes; UP000233100; Chromosome 2.
DR   Bgee; ENSMFAG00000040128; Expressed in frontal cortex and 4 other tissues.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR   GO; GO:0005883; C:neurofilament; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0008366; P:axon ensheathment; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0120192; P:tight junction assembly; IEA:Ensembl.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR003555; Claudin11.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; PTHR12002; 1.
DR   PANTHER; PTHR12002:SF6; PTHR12002:SF6; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01384; CLAUDIN11.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW   Tight junction; Transmembrane; Transmembrane helix.
FT   CHAIN           1..207
FT                   /note="Claudin-11"
FT                   /id="PRO_0000144761"
FT   TOPO_DOM        1
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        23..82
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..122
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..157
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..207
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99P82"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60771"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60771"
FT   MOD_RES         198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60771"
SQ   SEQUENCE   207 AA;  22004 MW;  66B4994578E900C8 CRC64;
     MVATCLQVVG FVTSFVGWIG VIVTTSTNDW VVTCGYTIPT CRKLDELGSK GLWADCVMAT
     GLYHCKPLVD ILILPGYVQA CRALMIAASV LGLPAILLLL TVLPCIRMGH EPGVAKYRRA
     QLAGVLLILL ALCAIVATIW FPVCAHRETT IVSFGYSLYA GWIGAVLCLV GGCVILCCAG
     DAQAFGENRF YYSSGSSSPT HAKSAHV