CLD10_PONAB
ID CLD10_PONAB Reviewed; 228 AA.
AC Q5R8E5; H2NK57; K7EV28;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Claudin-10;
GN Name=CLDN10;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) 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. Involved in the regulation of paracellular epithelia
CC permeability to ions in multiple organs. It acts as a paracellular ion
CC channel probably forming permselective pores; isoform 1 appears to
CC create pores preferentially permeable to cations and isoform 2 for
CC anions. In sweat glands and in the thick ascending limb (TAL) of
CC Henle's loop in kidney, it controls paracellular sodium permeability
CC which is essential for proper sweat production and renal function.
CC {ECO:0000250|UniProtKB:P78369}.
CC -!- SUBUNIT: Can form homodimers both in trans (interaction between CLDN10
CC molecules in opposing membranes) and in cis (interaction between CLDN10
CC molecules within one membrane). {ECO:0000250|UniProtKB:P78369}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P78369}. Cell membrane
CC {ECO:0000250|UniProtKB:P78369}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R8E5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R8E5-2; Sequence=VSP_053554;
CC -!- DOMAIN: The fourth transmembrane region (161-181) is necessary for
CC integration into tight junctions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91965.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR859807; CAH91965.1; ALT_FRAME; mRNA.
DR EMBL; ABGA01175643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01175660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q5R8E5; -.
DR SMR; Q5R8E5; -.
DR STRING; 9601.ENSPPYP00000006209; -.
DR Ensembl; ENSPPYT00000006454; ENSPPYP00000006209; ENSPPYG00000005449. [Q5R8E5-1]
DR Ensembl; ENSPPYT00000060673; ENSPPYP00000030226; ENSPPYG00000005449. [Q5R8E5-2]
DR eggNOG; ENOG502QPNP; Eukaryota.
DR GeneTree; ENSGT00940000155232; -.
DR InParanoid; Q5R8E5; -.
DR OrthoDB; 1164514at2759; -.
DR TreeFam; TF331936; -.
DR Proteomes; UP000001595; Chromosome 13.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0043269; P:regulation of ion transport; ISS:UniProtKB.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003554; Claudin10.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF13; PTHR12002:SF13; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01383; CLAUDIN10.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell junction; Cell membrane; Ion transport;
KW Membrane; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..228
FT /note="Claudin-10"
FT /id="PRO_0000144759"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..73
FT /note="MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKA
FT CVTDSTGVSNCKDFPSMLALD -> MSRAQIWALVSGVGGFGALVAATTSNEWKVTTRA
FT SSVITATWVYQGLWMNCAGNALGSFHCRPHFTIFKVA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053554"
FT CONFLICT 91
FT /note="F -> S (in Ref. 1; CAH91965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 24458 MW; 11E66F82A667B87B CRC64;
MASTASEIIA FMVSISGWVL VSSTLPTDYW KVSTIDGTVI TTATYWANLW KACVTDSTGV
SNCKDFPSML ALDGYIQACR GLMIAAVSLG FFGSIFALFG MKCTKVGGSD KAKAKIACLA
GIVFILSGLC SMTGCSLYAN KITTEFFDPL FVEQKYELGA ALFIGWAGAS LCIIGGVIFC
FSISDNNKTP RYAYNGATSV MSSRTKYHGG EDFKTTNPSK QFDKNAYV
