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CLD10_BOVIN
ID   CLD10_BOVIN             Reviewed;         231 AA.
AC   Q5E9L0; A7Z072;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Claudin-10;
GN   Name=CLDN10;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Hereford; TISSUE=Kidney;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2007) 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=Q5E9L0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5E9L0-2; Sequence=VSP_053549;
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}.
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DR   EMBL; BT020910; AAX08927.1; -; mRNA.
DR   EMBL; DAAA02034568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02034569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02034570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02034571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02034572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC153270; AAI53271.1; -; mRNA.
DR   RefSeq; NP_001014857.1; NM_001014857.1. [Q5E9L0-1]
DR   RefSeq; NP_001099079.1; NM_001105609.2. [Q5E9L0-2]
DR   AlphaFoldDB; Q5E9L0; -.
DR   SMR; Q5E9L0; -.
DR   STRING; 9913.ENSBTAP00000004641; -.
DR   PaxDb; Q5E9L0; -.
DR   Ensembl; ENSBTAT00000004641; ENSBTAP00000004641; ENSBTAG00000003568. [Q5E9L0-1]
DR   Ensembl; ENSBTAT00000056559; ENSBTAP00000048962; ENSBTAG00000003568. [Q5E9L0-2]
DR   GeneID; 506545; -.
DR   KEGG; bta:506545; -.
DR   CTD; 9071; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003568; -.
DR   eggNOG; ENOG502QPNP; Eukaryota.
DR   GeneTree; ENSGT00940000155232; -.
DR   HOGENOM; CLU_076370_0_0_1; -.
DR   InParanoid; Q5E9L0; -.
DR   OMA; CKEFISM; -.
DR   OrthoDB; 1164514at2759; -.
DR   TreeFam; TF331936; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000003568; Expressed in prostate gland and 83 other tissues.
DR   GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
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..231
FT                   /note="Claudin-10"
FT                   /id="PRO_0000244418"
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..231
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..73
FT                   /note="MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKT
FT                   CVTDSTGVSNCKDFPSMLALD -> MSRAQISALVFGVGGFGALVAATASNEWKVTTRA
FT                   SSVITATWVYQGLWMNCAGNALGSFHCRPHFTIFKVE (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_053549"
SQ   SEQUENCE   231 AA;  24761 MW;  84C4DE6C59DCAF9C CRC64;
     MASTASEIIA FMVSISGWVL VSSTLPTDYW KVSTIDGTVI TTATYWANLW KTCVTDSTGV
     SNCKDFPSML ALDGYIQACR GLMIAAVSLG FFGSIFALIG MKCTKVGGSD KAKAKIACLA
     GIVFILSGLC SMTGCSLYAN KITTEFFDPL FVEQKYELGA ALFIGWAGAS LCLIGGVIFC
     FSISDNNKAP RMGYTYNGAT SVMSSRTKYH GREGDLKTPN PSKQFDKNAY V
 
 
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