O88551 (CLD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Claudin-1

Gene names

Name:

Cldn1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Ref.4
Subunit structure	Can form homo- and heteropolymers with other CLDN. Homopolymers interact with CLDN3, but not CLDN2, homopolymers. Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. Interacts with MPDZ and INADL. Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Cell junction › tight junction. Cell membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Widely expressed, with highest levels in liver and kidney. Ref.1
Sequence similarities	Belongs to the claudin family.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Tight junction
Domain	Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	calcium-independent cell-cell adhesion Inferred from direct assay Ref.4. Source: UniProtKB cell-cell junction organization Inferred from electronic annotation. Source: Compara
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 20089884. Source: MGI integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB lateral plasma membrane Inferred from electronic annotation. Source: Compara tight junction Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 211	211	Claudin-1		PRO_0000144730
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 28	21	Helical; Potential
	Topological domain	29 – 81	53	Extracellular Potential
	Transmembrane	82 – 102	21	Helical; Potential
	Topological domain	103 – 115	13	Cytoplasmic Potential
	Transmembrane	116 – 136	21	Helical; Potential
	Topological domain	137 – 163	27	Extracellular Potential
	Transmembrane	164 – 184	21	Helical; Potential
	Topological domain	185 – 211	27	Cytoplasmic Potential
	Region	210 – 211	2	Interactions with TJP1, TJP2, TJP3 and INADL
Amino acid modifications
	Modified residue	205	1	Phosphoserine Ref.9
	Modified residue	206	1	Phosphoserine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	O88551 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: BEF896FA62DBB6F0	FASTA	211	22,881
	10 20 30 40 50 60 MANAGLQLLG FILASLGWIG SIVSTALPQW KIYSYAGDNI VTAQAIYEGL WMSCVSQSTG 70 80 90 100 110 120 QIQCKVFDSL LNLNSTLQAT RALMVIGILL GLIAIFVSTI GMKCMRCLED DEVQKMWMAV 130 140 150 160 170 180 IGGIIFLISG LATLVATAWY GNRIVQEFYD PLTPINARYE FGQALFTGWA AASLCLLGGV 190 200 210 LLSCSCPRKT TSYPTPRPYP KPTPSSGKDY V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin." Furuse M., Fujita K., Hiiragi T., Fujimoto K., Tsukita S. J. Cell Biol. 141:1539-1550(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Liver.
[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. , 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: Embryonic head, Liver, Oviduct, Thymus and Vagina.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
[4]	"Ca(2+)-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions." Kubota K., Furuse M., Sasaki H., Sonoda N., Fujita K., Nagafuchi A., Tsukita S. Curr. Biol. 9:1035-1038(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Manner of interaction of heterogeneous claudin species within and between tight junction strands." Furuse M., Sasaki H., Tsukita S. J. Cell Biol. 147:891-903(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CLDN2 AND CLDN3.
[6]	"Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins." Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S. J. Cell Biol. 147:1351-1363(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TJP1; TJP2 AND TJP3.
[7]	"Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions." Itoh M., Sasaki H., Furuse M., Ozaki H., Kita T., Tsukita S. J. Cell Biol. 154:491-497(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MPDZ.
[8]	"The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions." Roh M.H., Liu C.-J., Laurinec S., Margolis B. J. Biol. Chem. 277:27501-27509(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INADL.
[9]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-206, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF072127 mRNA. Translation: AAC27078.1. AK028428 mRNA. Translation: BAC25945.1. AK036762 mRNA. Translation: BAC29567.1. AK036780 mRNA. Translation: BAC29574.1. AK040604 mRNA. Translation: BAC30640.1. AK054207 mRNA. Translation: BAC35693.1. AK081601 mRNA. Translation: BAC38267.1. BC002003 mRNA. Translation: AAH02003.1.
IPI	IPI00131931.
RefSeq	NP_057883.1. NM_016674.4.
UniGene	Mm.289441.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-113174.
STRING	10090.ENSMUSP00000023154.
PTM databases
PhosphoSite	O88551.
Proteomic databases
PaxDb	O88551.
PRIDE	O88551.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023154; ENSMUSP00000023154; ENSMUSG00000022512.
GeneID	12737.
KEGG	mmu:12737.
Organism-specific databases
CTD	9076.
MGI	MGI:1276109. Cldn1.
Phylogenomic databases
eggNOG	NOG47316.
HOGENOM	HOG000220937.
HOVERGEN	HBG000643.
InParanoid	O88551.
KO	K06087.
OMA	IYEGLWM.
OrthoDB	EOG4G7C0B.
Enzyme and pathway databases
Reactome	REACT_137402. Cell-Cell communication.
Gene expression databases
ArrayExpress	O88551.
Bgee	O88551.
CleanEx	MM_CLDN1.
Genevestigator	O88551.
GermOnline	ENSMUSG00000022512. Mus musculus.
Family and domain databases
InterPro	IPR006187. Claudin. IPR003548. Claudin1. IPR017974. Claudin_CS. IPR004031. PMP22/EMP/MP20/Claudin. [Graphical view]
PANTHER	PTHR12002. PTHR12002. 1 hit. PTHR12002:SF29. PTHR12002:SF29. 1 hit.
Pfam	PF00822. PMP22_Claudin. 1 hit. [Graphical view]
PRINTS	PR01077. CLAUDIN. PR01377. CLAUDIN1.
PROSITE	PS01346. CLAUDIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	282042.
PMAP-CutDB	O88551.
SOURCE	Search...

Entry information

Entry name

CLD1_MOUSE

Accession

Primary (citable) accession number: O88551

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program