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CLD14_MOUSE
ID   CLD14_MOUSE             Reviewed;         239 AA.
AC   Q9Z0S3; Q9D284;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Claudin-14;
GN   Name=Cldn14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Morita K., Furuse M., Tsukita S.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=11163249; DOI=10.1016/s0092-8674(01)00200-8;
RA   Wilcox E.R., Burton Q.L., Naz S., Riazuddin S., Smith T.N., Ploplis B.,
RA   Belyantseva I., Ben-Yosef T., Liburd N.A., Morell R.J., Kachar B., Wu D.K.,
RA   Griffith A.J., Riazuddin S., Friedman T.B.;
RT   "Mutations in the gene encoding tight junction claudin-14 cause autosomal
RT   recessive deafness DFNB29.";
RL   Cell 104:165-172(2001).
RN   [3]
RP   SEQUENCE REVISION TO 115; 129; 166 AND 187.
RA   Wilcox E.R., Burton Q.L., Naz S., Riazuddin S., Smith T.N., Ploplis B.,
RA   Belyantseva I., Ben-Yosef T., Liburd N.A., Morell R.J., Kachar B., Wu D.K.,
RA   Griffith A.J., Riazuddin S., Friedman T.B.;
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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   -!- INTERACTION:
CC       Q9Z0S3; Q9Y5I7: CLDN16; Xeno; NbExp=3; IntAct=EBI-7774956, EBI-7774981;
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane;
CC       Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in all sensory epithelia of the inner ear
CC       vestibular organs, as well as in liver and kidney.
CC       {ECO:0000269|PubMed:11163249}.
CC   -!- DEVELOPMENTAL STAGE: At postnatal day 4, expression is apically located
CC       in the inner and outer hair cell region of the entire organ of Corti.
CC       By postnatal day 8, expression is highest in the supporting cells of
CC       the organ of Corti.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR   EMBL; AF124429; AAD17323.1; -; mRNA.
DR   EMBL; AF314089; AAG60051.2; -; mRNA.
DR   EMBL; AK020255; BAB32041.1; -; mRNA.
DR   CCDS; CCDS28345.1; -.
DR   RefSeq; NP_001159397.1; NM_001165925.1.
DR   RefSeq; NP_001159398.1; NM_001165926.1.
DR   RefSeq; NP_062373.3; NM_019500.4.
DR   RefSeq; XP_006523130.1; XM_006523067.3.
DR   AlphaFoldDB; Q9Z0S3; -.
DR   SMR; Q9Z0S3; -.
DR   IntAct; Q9Z0S3; 2.
DR   MINT; Q9Z0S3; -.
DR   STRING; 10090.ENSMUSP00000062045; -.
DR   iPTMnet; Q9Z0S3; -.
DR   PhosphoSitePlus; Q9Z0S3; -.
DR   PaxDb; Q9Z0S3; -.
DR   PRIDE; Q9Z0S3; -.
DR   Antibodypedia; 23104; 258 antibodies from 32 providers.
DR   DNASU; 56173; -.
DR   Ensembl; ENSMUST00000050962; ENSMUSP00000062045; ENSMUSG00000047109.
DR   Ensembl; ENSMUST00000169391; ENSMUSP00000126455; ENSMUSG00000047109.
DR   Ensembl; ENSMUST00000177648; ENSMUSP00000136156; ENSMUSG00000047109.
DR   GeneID; 56173; -.
DR   KEGG; mmu:56173; -.
DR   UCSC; uc008aad.2; mouse.
DR   CTD; 23562; -.
DR   MGI; MGI:1860425; Cldn14.
DR   VEuPathDB; HostDB:ENSMUSG00000047109; -.
DR   eggNOG; ENOG502QR8Z; Eukaryota.
DR   GeneTree; ENSGT00940000161312; -.
DR   HOGENOM; CLU_076370_1_1_1; -.
DR   InParanoid; Q9Z0S3; -.
DR   OMA; PHWRRTS; -.
DR   OrthoDB; 1309858at2759; -.
DR   PhylomeDB; Q9Z0S3; -.
DR   TreeFam; TF331936; -.
DR   BioGRID-ORCS; 56173; 1 hit in 74 CRISPR screens.
DR   PRO; PR:Q9Z0S3; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9Z0S3; protein.
DR   Bgee; ENSMUSG00000047109; Expressed in lumbar subsegment of spinal cord and 100 other tissues.
DR   ExpressionAtlas; Q9Z0S3; baseline and differential.
DR   Genevisible; Q9Z0S3; MM.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
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: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   InterPro; IPR006187; Claudin.
DR   InterPro; IPR003556; Claudin14.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; PTHR12002; 1.
DR   PANTHER; PTHR12002:SF99; PTHR12002:SF99; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Membrane; Reference proteome; Tight junction;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..239
FT                   /note="Claudin-14"
FT                   /id="PRO_0000144770"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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..162
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..239
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        115
FT                   /note="T -> N (in Ref. 1; AAD17323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="V -> M (in Ref. 4; BAB32041)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="G -> A (in Ref. 1; AAD17323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="L -> M (in Ref. 1; AAD17323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="D -> E (in Ref. 1; AAD17323)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   239 AA;  25614 MW;  24DE6AEADA56BB61 CRC64;
     MASTAVQLLG FLLSFLGMVG TLITTILPHW RRTAHVGTNI LTAVSYLKGL WMECVWHSTG
     IYQCQIYRSL LALPRDLQAA RALMVISCLL SGMACACAVV GMKCTRCAKG TPAKTTFAVL
     GGALFLLAGL LCMVAVSWTT NDVVQNFYNP LLPSGMKFEI GQALYLGFIS SSLSLIGGTL
     LCLSCQDEAP YRPYPPQSRA GATTTATAPA YRPPAAYKDN RAPSVTSAAH SGYRLNDYV
 
 
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