位置:首页 > 蛋白库 > CLD15_HUMAN
CLD15_HUMAN
ID   CLD15_HUMAN             Reviewed;         228 AA.
AC   P56746; B3KPB5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Claudin-15;
GN   Name=CLDN15;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Keen T.J., Inglehearn C.F.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   GLU-46; ASP-55 AND GLU-64.
RX   PubMed=12055082; DOI=10.1152/ajpcell.00038.2002;
RA   Colegio O.R., Van Itallie C.M., McCrea H.J., Rahner C., Anderson J.M.;
RT   "Claudins create charge-selective channels in the paracellular pathway
RT   between epithelial cells.";
RL   Am. J. Physiol. 283:C142-C147(2002).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=13129853; DOI=10.1152/ajprenal.00116.2003;
RA   Van Itallie C.M., Fanning A.S., Anderson J.M.;
RT   "Reversal of charge selectivity in cation or anion-selective epithelial
RT   lines by expression of different claudins.";
RL   Am. J. Physiol. 285:F1078-F1084(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
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 function as impermeable barriers, others mediate
CC       the permeability to ions and small molecules. Often, several claudin
CC       family members are coexpressed and interact with each other, and this
CC       determines the overall permeability. CLDN15 forms tight junctions that
CC       mediate the paracellular transport of small monovalent cations along a
CC       concentration gradient, due to selective permeability for Na(+), Li(+)
CC       and K(+) ions, but selects against Cl(-) ions. Plays an important role
CC       in paracellular Na(+) transport in the intestine and in Na(+)
CC       homeostasis. Required for normal Na(+)-dependent intestinal nutrient
CC       uptake. {ECO:0000269|PubMed:12055082, ECO:0000269|PubMed:13129853}.
CC   -!- SUBUNIT: Can form linear homooligomers in the membrane, giving rise to
CC       tight junction strand-like structures.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane;
CC       Multi-pass membrane protein. Note=Tight junctions form continuous
CC       circumferential cell-cell contacts at the borders of apical and lateral
CC       cell membranes that seal the intercellular space and show up as strand-
CC       like structures in electron microscopy.
CC   -!- TISSUE SPECIFICITY: Detected in colon (at protein level).
CC       {ECO:0000269|PubMed:12055082}.
CC   -!- PTM: Palmitoylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ245738; CAB52587.1; -; mRNA.
DR   EMBL; AK056103; BAG51627.1; -; mRNA.
DR   EMBL; CH471197; EAW50211.1; -; Genomic_DNA.
DR   CCDS; CCDS5717.1; -.
DR   RefSeq; NP_001172009.1; NM_001185080.1.
DR   RefSeq; NP_055158.1; NM_014343.2.
DR   AlphaFoldDB; P56746; -.
DR   SMR; P56746; -.
DR   BioGRID; 117296; 4.
DR   IntAct; P56746; 1.
DR   STRING; 9606.ENSP00000385300; -.
DR   TCDB; 1.H.1.1.9; the claudin tight junction (claudin1) family.
DR   iPTMnet; P56746; -.
DR   PhosphoSitePlus; P56746; -.
DR   BioMuta; CLDN15; -.
DR   DMDM; 6685306; -.
DR   jPOST; P56746; -.
DR   MassIVE; P56746; -.
DR   PaxDb; P56746; -.
DR   PeptideAtlas; P56746; -.
DR   PRIDE; P56746; -.
DR   ProteomicsDB; 56942; -.
DR   Antibodypedia; 16744; 201 antibodies from 21 providers.
DR   DNASU; 24146; -.
DR   Ensembl; ENST00000308344.10; ENSP00000308870.5; ENSG00000106404.14.
DR   Ensembl; ENST00000401528.5; ENSP00000385300.1; ENSG00000106404.14.
DR   GeneID; 24146; -.
DR   KEGG; hsa:24146; -.
DR   MANE-Select; ENST00000308344.10; ENSP00000308870.5; NM_014343.3; NP_055158.1.
DR   UCSC; uc003uyg.2; human.
DR   CTD; 24146; -.
DR   DisGeNET; 24146; -.
DR   GeneCards; CLDN15; -.
DR   HGNC; HGNC:2036; CLDN15.
DR   HPA; ENSG00000106404; Tissue enriched (intestine).
DR   MIM; 615778; gene.
DR   neXtProt; NX_P56746; -.
DR   OpenTargets; ENSG00000106404; -.
DR   PharmGKB; PA26562; -.
DR   VEuPathDB; HostDB:ENSG00000106404; -.
DR   eggNOG; ENOG502RYAR; Eukaryota.
DR   GeneTree; ENSGT00940000157650; -.
DR   InParanoid; P56746; -.
DR   OMA; FYPGIKY; -.
DR   OrthoDB; 1375597at2759; -.
DR   PhylomeDB; P56746; -.
DR   TreeFam; TF331936; -.
DR   PathwayCommons; P56746; -.
DR   Reactome; R-HSA-420029; Tight junction interactions.
DR   SignaLink; P56746; -.
DR   BioGRID-ORCS; 24146; 19 hits in 1079 CRISPR screens.
DR   GeneWiki; CLDN15; -.
DR   GenomeRNAi; 24146; -.
DR   Pharos; P56746; Tbio.
DR   PRO; PR:P56746; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P56746; protein.
DR   Bgee; ENSG00000106404; Expressed in jejunal mucosa and 137 other tissues.
DR   ExpressionAtlas; P56746; baseline and differential.
DR   Genevisible; P56746; HS.
DR   GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR008094; Claudin15.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; PTHR12002; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01718; CLAUDIN15.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Disulfide bond; Ion transport; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Reference proteome; Tight junction;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..228
FT                   /note="Claudin-15"
FT                   /id="PRO_0000144771"
FT   TOPO_DOM        1
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        2..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        25..74
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        75..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        100..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        116..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        141..159
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        160..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        183..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          146..147
FT                   /note="Important for the formation of tight-junction
FT                   strand-like structures"
FT                   /evidence="ECO:0000250"
FT   REGION          208..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            55
FT                   /note="Important for Na(+)-selective paracellular ion
FT                   transport"
FT   SITE            64
FT                   /note="Important for Na(+)-selective paracellular ion
FT                   transport"
FT   SITE            68
FT                   /note="Important for the formation of tight-junction
FT                   strand-like structures"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D3ZQJ0"
FT   MOD_RES         218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z0S5"
FT   DISULFID        52..62
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         46
FT                   /note="E->K: No effect on charge selectivity for
FT                   paracellular ion transport."
FT                   /evidence="ECO:0000269|PubMed:12055082"
FT   MUTAGEN         55
FT                   /note="D->R: Reverses the charge selectivity for
FT                   paracellular ion transport, favoring Cl(-) transport."
FT                   /evidence="ECO:0000269|PubMed:12055082"
FT   MUTAGEN         64
FT                   /note="E->K: Impairs the charge selectivity for
FT                   paracellular ion transport, favoring Cl(-) transport."
FT                   /evidence="ECO:0000269|PubMed:12055082"
SQ   SEQUENCE   228 AA;  24356 MW;  D502E2CD9116F4B1 CRC64;
     MSMAVETFGF FMATVGLLML GVTLPNSYWR VSTVHGNVIT TNTIFENLWF SCATDSLGVY
     NCWEFPSMLA LSGYIQACRA LMITAILLGF LGLLLGIAGL RCTNIGGLEL SRKAKLAATA
     GALHILAGIC GMVAISWYAF NITRDFFDPL YPGTKYELGP ALYLGWSASL ISILGGLCLC
     SACCCGSDED PAASARRPYQ APVSVMPVAT SDQEGDSSFG KYGRNAYV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024