CLD11_RAT
ID CLD11_RAT Reviewed; 207 AA.
AC Q99P82;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Claudin-11;
GN Name=Cldn11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11316752; DOI=10.1210/endo.142.5.8116;
RA Lui W.Y., Lee W.M., Cheng C.Y.;
RT "Transforming growth factor-beta3 perturbs the inter-Sertoli tight junction
RT permeability barrier in vitro possibly mediated via its effects on
RT occludin, zonula occludens-1, and claudin-11.";
RL Endocrinology 142:1865-1877(2001).
RN [2]
RP PROTEIN SEQUENCE OF 44-50 AND 190-203, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-194; SER-197 AND
RP SER-198, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Cell membrane
CC {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; AF324043; AAG50277.1; -; mRNA.
DR AlphaFoldDB; Q99P82; -.
DR SMR; Q99P82; -.
DR IntAct; Q99P82; 1.
DR MINT; Q99P82; -.
DR STRING; 10116.ENSRNOP00000014359; -.
DR iPTMnet; Q99P82; -.
DR PhosphoSitePlus; Q99P82; -.
DR PaxDb; Q99P82; -.
DR PRIDE; Q99P82; -.
DR UCSC; RGD:71081; rat.
DR RGD; 71081; Cldn11.
DR eggNOG; ENOG502QSDJ; Eukaryota.
DR InParanoid; Q99P82; -.
DR PhylomeDB; Q99P82; -.
DR PRO; PR:Q99P82; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0045178; C:basal part of cell; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005883; C:neurofilament; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0070160; C:tight junction; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008366; P:axon ensheathment; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0120192; P:tight junction assembly; ISO:RGD.
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 1: Evidence at protein level;
KW Cell junction; Cell membrane; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..207
FT /note="Claudin-11"
FT /id="PRO_0000144764"
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:0007744|PubMed:22673903"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 207 AA; 22046 MW; C71B8D34E2355C41 CRC64;
MVATCLQVVG FVTSFVGWIG IIVTTSTNDW VVTCSYTIPT CRKMDELGSK GLWADCVMAT
GLHHCKPLVD ILILPGYAQA CRALMIAASV LGLPGILLLL TVLPCIRMGH EPGVAKYRRA
QLAGVLLILL ALCAIVATIW FPVCAHREIT IVSFGYSLYA GWIGAVMCLV GGCVIVCCSG
DAQSFGENRF YYSSGSSSPT HAKSAHV
