ID   A0A2K5E1N5_AOTNA        Unreviewed;       207 AA.
AC   A0A2K5E1N5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN   Name=CLDN11 {ECO:0000313|Ensembl:ENSANAP00000027160.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000027160.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000027160.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC       the intercellular space, through calcium-independent cell-adhesion
CC       activity. {ECO:0000256|ARBA:ARBA00002246,
CC       ECO:0000256|RuleBase:RU060637}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|RuleBase:RU060637}. Cell membrane
CC       {ECO:0000256|RuleBase:RU060637}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU060637}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the claudin family.
CC       {ECO:0000256|ARBA:ARBA00008295, ECO:0000256|RuleBase:RU060637}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU060637}.
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DR   AlphaFoldDB; A0A2K5E1N5; -.
DR   STRING; 37293.ENSANAP00000027160; -.
DR   Ensembl; ENSANAT00000045150.1; ENSANAP00000027160.1; ENSANAG00000031372.1.
DR   GeneTree; ENSGT00890000139496; -.
DR   OMA; SYQDNNH; -.
DR   OrthoDB; 4604546at2759; -.
DR   Proteomes; UP000233020; Unplaced.
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: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   Gene3D; 1.20.140.150; -; 1.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR003555; Claudin11.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; CLAUDIN; 1.
DR   PANTHER; PTHR12002:SF6; CLAUDIN-11; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PRINTS; PR01384; CLAUDIN11.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949,
KW   ECO:0000256|RuleBase:RU060637};
KW   Cell membrane {ECO:0000256|RuleBase:RU060637};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU060637};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW   Tight junction {ECO:0000256|ARBA:ARBA00022427,
KW   ECO:0000256|RuleBase:RU060637};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU060637};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU060637}.
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        124..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        155..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
SQ   SEQUENCE   207 AA;  21994 MW;  E580AC882A2069F2 CRC64;
     MVATCLQVVG FVTSFVGWIG IIVTTSTNDW VVTCGYTIPT CRKLDELGSK GLWADCVMAT
     GLYHCKPLVD ILILPGYVQA CRALMIAASV LGLPAILLLL TVLPCIRMGR EPGVAKYRRA
     QLAGVLLILL ALCAIVATIW FPVCAHRETT IVSFGYSLYA GWIGAVLCLV GGCVILCCAG
     DAQSFGENPF YYSSGSSSPT HAKSAHV
//