CLD1_BOVIN
ID CLD1_BOVIN Reviewed; 211 AA.
AC Q6L708; Q3ZC38;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Claudin-1;
GN Name=CLDN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Ohta H., Takiguchi M., Inaba M.;
RT "Localization of claudin proteins in bovine kidneys.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Rumen reticulum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Claudins function as major constituents of the tight junction
CC complexes that regulate the permeability of epithelia. While some
CC claudin family members play essential roles in the formation of
CC impermeable barriers, others mediate the permeability to ions and small
CC molecules. Often, several claudin family members are coexpressed and
CC interact with each other, and this determines the overall permeability.
CC CLDN1 is required to prevent the paracellular diffusion of small
CC molecules through tight junctions in the epidermis and is required for
CC the normal barrier function of the skin. Required for normal water
CC homeostasis and to prevent excessive water loss through the skin,
CC probably via an indirect effect on the expression levels of other
CC proteins, since CLDN1 itself seems to be dispensable for water barrier
CC formation in keratinocyte tight junctions (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Can form homo- and heteropolymers with other CLDN.
CC Homopolymers interact with CLDN3, but not CLDN2, homopolymers.
CC Interacts with MPDZ and PATJ. Interacts with OCLN, CD81, CLDN4, CLDN6
CC and CLDN9. {ECO:0000250|UniProtKB:O88551,
CC ECO:0000250|UniProtKB:O95832}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:O95832}. Cell membrane
CC {ECO:0000250|UniProtKB:O95832}; Multi-pass membrane protein
CC {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:O95832}. Note=Associates with CD81 and the
CC CLDN1-CD81 complex localizes to the basolateral cell membrane.
CC {ECO:0000250|UniProtKB:O95832}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AB178476; BAD21101.1; -; mRNA.
DR EMBL; BT021861; AAX46708.1; -; mRNA.
DR EMBL; BC102930; AAI02931.1; -; mRNA.
DR RefSeq; NP_001001854.1; NM_001001854.2.
DR AlphaFoldDB; Q6L708; -.
DR SMR; Q6L708; -.
DR STRING; 9913.ENSBTAP00000017476; -.
DR PaxDb; Q6L708; -.
DR Ensembl; ENSBTAT00000017476; ENSBTAP00000017476; ENSBTAG00000013148.
DR GeneID; 414922; -.
DR KEGG; bta:414922; -.
DR CTD; 9076; -.
DR VEuPathDB; HostDB:ENSBTAG00000013148; -.
DR VGNC; VGNC:27402; CLDN1.
DR eggNOG; ENOG502R7HF; Eukaryota.
DR GeneTree; ENSGT00940000155387; -.
DR HOGENOM; CLU_076370_2_3_1; -.
DR InParanoid; Q6L708; -.
DR OMA; CCCPQKA; -.
DR OrthoDB; 1244077at2759; -.
DR TreeFam; TF331936; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000013148; Expressed in myometrium and 93 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; ISS:AgBase.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; ISS:AgBase.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0001618; F:virus receptor activity; IEA:Ensembl.
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:AgBase.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0034331; P:cell junction maintenance; IEA:Ensembl.
DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEA:Ensembl.
DR GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:Ensembl.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003548; Claudin1.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF92; PTHR12002:SF92; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01377; CLAUDIN1.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Membrane; Reference proteome;
KW Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..211
FT /note="Claudin-1"
FT /id="PRO_0000144728"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..211
FT /note="Interactions with TJP1, TJP2, TJP3 and PATJ"
FT /evidence="ECO:0000250"
FT DISULFID 54..64
FT /evidence="ECO:0000250"
SQ SEQUENCE 211 AA; 22865 MW; D7BADCC2E9010FBB CRC64;
MANAGLQLLG FILAFLGWIG SIVSTALPQW KVYSYASDNI VTAQAIYEGL WMSCVSQSTG
QIQCKVFDSL LNLNSTLQAT RALMVIGILL GLIAIFVATV GMKCMKCMED DEAQKMRMAV
FGGVIFLISG LAILVATAWY GNRIVQEFYD PMTPVNARYE FGQALFIGWA AASLCLLGGA
LLCCSCPRKT TSYPTPRPYP KPAPSSGKDY V
