ID   CLD1_RAT                Reviewed;         211 AA.
AC   P56745; Q6P6V9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Claudin-1;
GN   Name=Cldn1;
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], VARIANT ASP-23, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=11159859; DOI=10.1210/endo.142.2.7975;
RA   Gregory M., Dufresne J., Hermo L., Cyr D.;
RT   "Claudin-1 is not restricted to tight junctions in the rat epididymis.";
RL   Endocrinology 142:854-863(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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. Directly
CC       interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. Interacts with MPDZ
CC       and PATJ. Interacts with OCLN, CD81, CLDN4, CLDN6 and CLDN9.
CC       {ECO:0000250|UniProtKB:O88551, ECO:0000250|UniProtKB:O95832}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000269|PubMed:11159859}. Cell membrane
CC       {ECO:0000269|PubMed:11159859}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11159859}. 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   -!- TISSUE SPECIFICITY: Detected in epididymis (at protein level). Detected
CC       in testis and epididymis. {ECO:0000269|PubMed:11159859}.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR   EMBL; AF195500; AAF04850.1; -; mRNA.
DR   EMBL; BC061992; AAH61992.1; -; mRNA.
DR   RefSeq; NP_113887.2; NM_031699.2.
DR   AlphaFoldDB; P56745; -.
DR   SMR; P56745; -.
DR   STRING; 10116.ENSRNOP00000002640; -.
DR   iPTMnet; P56745; -.
DR   PhosphoSitePlus; P56745; -.
DR   PaxDb; 10116-ENSRNOP00000002640; -.
DR   Ensembl; ENSRNOT00000002640.6; ENSRNOP00000002640.3; ENSRNOG00000001926.7.
DR   Ensembl; ENSRNOT00055007277; ENSRNOP00055005439; ENSRNOG00055004594.
DR   Ensembl; ENSRNOT00060022222; ENSRNOP00060017609; ENSRNOG00060013046.
DR   GeneID; 65129; -.
DR   KEGG; rno:65129; -.
DR   UCSC; RGD:68422; rat.
DR   AGR; RGD:68422; -.
DR   CTD; 9076; -.
DR   RGD; 68422; Cldn1.
DR   eggNOG; ENOG502R7HF; Eukaryota.
DR   GeneTree; ENSGT00940000155387; -.
DR   HOGENOM; CLU_076370_2_3_1; -.
DR   InParanoid; P56745; -.
DR   OMA; CCCPQKA; -.
DR   OrthoDB; 4040914at2759; -.
DR   PhylomeDB; P56745; -.
DR   TreeFam; TF331936; -.
DR   PRO; PR:P56745; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000001926; Expressed in liver and 18 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
DR   GO; GO:0030054; C:cell junction; ISO:RGD.
DR   GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; 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:0001618; F:virus receptor activity; ISO:RGD.
DR   GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
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; IBA:GO_Central.
DR   GO; GO:0034331; P:cell junction maintenance; ISO:RGD.
DR   GO; GO:0045216; P:cell-cell junction organization; ISO:RGD.
DR   GO; GO:1903545; P:cellular response to butyrate; IEP:RGD.
DR   GO; GO:0071284; P:cellular response to lead ion; IEP:RGD.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR   GO; GO:0071346; P:cellular response to type II interferon; IEP:RGD.
DR   GO; GO:0008065; P:establishment of blood-nerve barrier; IMP:RGD.
DR   GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:RGD.
DR   GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR   GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR   GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; IMP:RGD.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR   GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISO:RGD.
DR   GO; GO:0090303; P:positive regulation of wound healing; ISO:RGD.
DR   GO; GO:0051259; P:protein complex oligomerization; ISO:RGD.
DR   GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0070673; P:response to interleukin-18; IMP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR   GO; GO:0061772; P:xenobiotic transport across blood-nerve barrier; IMP:RGD.
DR   Gene3D; 1.20.140.150; -; 1.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR003548; Claudin1.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; CLAUDIN; 1.
DR   PANTHER; PTHR12002:SF92; CLAUDIN-1; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PRINTS; PR01377; CLAUDIN1.
DR   PROSITE; PS01346; CLAUDIN; 1.
DR   Genevisible; P56745; RN.
PE   1: Evidence at protein 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_0000144731"
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..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..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          190..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"
FT   VARIANT         23
FT                   /note="V -> D"
FT                   /evidence="ECO:0000269|PubMed:11159859"
FT   CONFLICT        133
FT                   /note="T -> I (in Ref. 1; AAF04850)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="V -> I (in Ref. 2; AAH61992)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="S -> T (in Ref. 2; AAH61992)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   211 AA;  22843 MW;  5B123CE46C110D97 CRC64;
     MANAGLQLLG FILASLGWIG SIVSTALPQW KIYSYAGDNI VTAQAIYEGL WMSCVSQSTG
     QIQCKVFDSL LNLNSTLQAT RALMVIGILL GLIAIFVSTI GMKCMRCLED DEVQKMWMAV
     IGGIIFVISG LATLVATAWY GNRIVQEFYD PMTPVNARYE FGQALFTGWA AASLCLLGGA
     LLSCSCPRKT TSYPTPRPYP KPTPSSGKDY V
//