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Q925N4 (CLD16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Claudin-16
Alternative name(s):
Paracellin-1
Gene names
Name:Cldn16
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors By similarity.

Subcellular location

Cell junctiontight junction. Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the claudin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 235235Claudin-16
PRO_0000144775

Regions

Topological domain1 – 33Cytoplasmic Potential
Transmembrane4 – 2421Helical; Potential
Topological domain25 – 7955Extracellular Potential
Transmembrane80 – 10021Helical; Potential
Topological domain101 – 11515Cytoplasmic Potential
Transmembrane116 – 13621Helical; Potential
Topological domain137 – 16933Extracellular Potential
Transmembrane170 – 19021Helical; Potential
Topological domain191 – 23545Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
Q925N4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C0601A64D87891FF

FASTA23526,100
        10         20         30         40         50         60 
MKDLLQYAAC FLAIFSTGFL IVATWTDCWM VNADDSLEVS TKCRGLWWEC VTNAFDGIRT 

        70         80         90        100        110        120 
CDEYDSIYAE HPLKLVVTRA LMITADILAG FGFITLLLGL DCVKFLPDDP QIKVRLCFVA 

       130        140        150        160        170        180 
GTTLLIAGTP GIIGSVWYAV DVYVERSSLV LHNIFLGIQY KFGWSCWLGM AGSLGCFLAG 

       190        200        210        220        230 
ALLTCCLYLF KDVGPERNYP YAMRKPYSTA GVSMAKSYKA PRTETAKMYA VDTRV 

« Hide

References

« Hide 'large scale' references
[1]"Primary gene structure and expression studies of rodent paracellin-1."
Weber S., Schlingmann K.P., Peters M., Nejsum L.N., Nielsen S., Engel H., Grzeschik K.H., Seyberth H.W., Grone H.J., Nusing R., Konrad M.
J. Am. Soc. Nephrol. 12:2664-2672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF323748 mRNA. Translation: AAK49518.1.
AK085268 mRNA. Translation: BAC39406.1.
AK085333 mRNA. Translation: BAC39425.1.
RefSeqNP_444471.1. NM_053241.5.
UniGeneMm.275205.

3D structure databases

ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ925N4.

Proteomic databases

PRIDEQ925N4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000115302; ENSMUSP00000110957; ENSMUSG00000038148.
ENSMUST00000161053; ENSMUSP00000124528; ENSMUSG00000038148.
GeneID114141.
KEGGmmu:114141.
UCSCuc007yva.2. mouse.

Organism-specific databases

CTD10686.
MGIMGI:2148742. Cldn16.

Phylogenomic databases

eggNOGNOG38970.
GeneTreeENSGT00730000111162.
HOGENOMHOG000111787.
HOVERGENHBG050987.
InParanoidQ925N4.
KOK06087.
OMAYAVDTRV.
OrthoDBEOG76HQ2T.
PhylomeDBQ925N4.
TreeFamTF331936.

Gene expression databases

BgeeQ925N4.
CleanExMM_CLDN16.
GenevestigatorQ925N4.

Family and domain databases

InterProIPR006187. Claudin.
IPR003927. Claudin16.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERPTHR12002. PTHR12002. 1 hit.
PTHR12002:SF56. PTHR12002:SF56. 1 hit.
PfamPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSPR01077. CLAUDIN.
PR01447. CLAUDIN16.
PROSITEPS01346. CLAUDIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio368133.
PROQ925N4.
SOURCESearch...

Entry information

Entry nameCLD16_MOUSE
AccessionPrimary (citable) accession number: Q925N4
Secondary accession number(s): Q542L7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot