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Protein

Cadherin-related family member 5

Gene

Cdhr5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Intermicrovillar adhesion molecule that forms, via its extracellular domain, calcium-dependent heterophilic complexes with CDHR2 on adjacent microvilli. Thereby, controls the packing of microvilli at the apical membrane of epithelial cells. Through its cytoplasmic domain, interacts with microvillus cytoplasmic proteins to form the intermicrovillar adhesion complex/IMAC. This complex plays a central role in microvilli and epithelial brush border differentiation.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-related family member 5Curated
Alternative name(s):
Mu-protocadherinImported
Gene namesi
Name:Cdhr5Imported
Synonyms:MucdhlImported, MupcdhImported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1919290. Cdhr5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 641613ExtracellularSequence analysisAdd
BLAST
Transmembranei642 – 66221HelicalSequence analysisAdd
BLAST
Topological domaini663 – 831169CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 831803Cadherin-related family member 5PRO_0000004013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...)Curated
Glycosylationi45 – 451N-linked (GlcNAc...)Curated
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence analysis
Glycosylationi135 – 1351N-linked (GlcNAc...)Curated
Glycosylationi143 – 1431N-linked (GlcNAc...)Curated
Glycosylationi173 – 1731N-linked (GlcNAc...)Curated
Glycosylationi201 – 2011N-linked (GlcNAc...)Curated
Glycosylationi287 – 2871N-linked (GlcNAc...)Curated
Glycosylationi311 – 3111N-linked (GlcNAc...)Curated
Glycosylationi408 – 4081N-linked (GlcNAc...)Curated
Glycosylationi475 – 4751N-linked (GlcNAc...)Curated
Modified residuei699 – 6991PhosphoserineBy similarity
Modified residuei721 – 7211PhosphoserineCombined sources
Modified residuei725 – 7251PhosphoserineCombined sources
Modified residuei728 – 7281PhosphothreonineCombined sources
Modified residuei736 – 7361PhosphoserineCombined sources
Modified residuei753 – 7531PhosphoserineCombined sources
Modified residuei795 – 7951PhosphothreonineBy similarity
Modified residuei802 – 8021PhosphoserineBy similarity
Modified residuei804 – 8041PhosphoserineBy similarity
Modified residuei806 – 8061PhosphoserineBy similarity

Post-translational modificationi

N- and O-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8VHF2.
PaxDbiQ8VHF2.
PRIDEiQ8VHF2.

PTM databases

iPTMnetiQ8VHF2.
PhosphoSiteiQ8VHF2.

Expressioni

Developmental stagei

Detected at embryonic day 7. Expression decreases by day 11 and increases again between embryonic days 15 and 17.1 Publication

Gene expression databases

BgeeiQ8VHF2.
CleanExiMM_MUPCDH.
ExpressionAtlasiQ8VHF2. baseline and differential.
GenevisibleiQ8VHF2. MM.

Interactioni

Subunit structurei

Part of the IMAC/intermicrovillar adhesion complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B, USH1C, CDHR2 and CDHR5. Interacts (via cytoplasmic domain) with USH1C and MYO7B; required for proper localization of CDHR5 to microvilli tips and its function in brush border differentiation.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000127292.

Structurei

3D structure databases

ProteinModelPortaliQ8VHF2.
SMRiQ8VHF2. Positions 70-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 12573Cadherin 1PROSITE-ProRule annotationCuratedAdd
BLAST
Domaini128 – 240113Cadherin 2PROSITE-ProRule annotationCuratedAdd
BLAST
Domaini252 – 357106Cadherin 3PROSITE-ProRule annotationCuratedAdd
BLAST
Domaini358 – 459102Cadherin 4PROSITE-ProRule annotationCuratedAdd
BLAST
Repeati541 – 571311CuratedAdd
BLAST
Repeati572 – 602312CuratedAdd
BLAST
Repeati605 – 614103; truncated

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni541 – 614743 X 31 AA approximate tandem repeatsAdd
BLAST
Regioni663 – 831169Mediates interaction with USH1C and MYO7B and is required for proper localization to microvilli tips and function in microvilli organizationBy similarityAdd
BLAST

Sequence similaritiesi

Contains 4 cadherin domains.PROSITE-ProRule annotationCurated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00390000001008.
HOGENOMiHOG000113693.
HOVERGENiHBG052536.
InParanoidiQ8VHF2.
KOiK16505.
PhylomeDBiQ8VHF2.

Family and domain databases

Gene3Di2.60.40.60. 2 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR030326. Mucdhl.
[Graphical view]
PANTHERiPTHR24027:SF313. PTHR24027:SF313. 1 hit.
SMARTiSM00112. CA. 2 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 2 hits.
PROSITEiPS00232. CADHERIN_1. 1 hit.
PS50268. CADHERIN_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: Q8VHF2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGAPALLWPS LLLPWLTVLF GQPPGTLAQT QVCSVNQTIF RVEENTTVSE
60 70 80 90 100
PLVNIFVPDG LHVTLGPLST PYAFRIEGKD LFLNVTPDYE ENSLLQADVE
110 120 130 140 150
CKRGDAVVVR LEVFVAVLDI NDNAPKFSFE IKTFNVSEDT KVNTTVIPET
160 170 180 190 200
QLKATDADIN DILVYTLQEV TPNASKFFSL EGVNYPALKL DQTLDYFKNQ
210 220 230 240 250
NMTFMLLARD TWEENVEPSH TATATLVLNT LPADLRTPWF LPCSFTDGYV
260 270 280 290 300
CIHAQYSAVV PTGHKLPSPL IMSPGPIYAV DGDQAINQSI IYSIIAGNTD
310 320 330 340 350
GTFIINAHDG NLTMTKSIPS PMKFTLLIRA DQEDMAQYSV TQAIVEARSV
360 370 380 390 400
TGNPLQFSQS LYYGTVVLGS EAGTAVKDKT FPSEILRIQA QYPGFPDLNS
410 420 430 440 450
AVTYRVTNSS EFMMNKDIML TAVPMEEART IRVEVEASNT VTKDTATAVV
460 470 480 490 500
EIQVSERERT PTPPEAGGTT GPSSNTTMEA PLTSGTSQRP ATTSSGGSVG
510 520 530 540 550
PFPPGGTTLR PPTPASSIPG GSPTLGTSTS PQTTTPGGDS AQTPKPGTSH
560 570 580 590 600
PTAPTSRTST SLMTTSSRSD STQTPKPGTS QPMVPIPGAS TSSQPATPSG
610 620 630 640 650
SSPQTPKPGT SQSTATGPIS LPSTGAGEQG DGQRFSTVDM AVLGGVLGAL
660 670 680 690 700
LLLALICLVI LVHKHYRHRL ACCSGKASEP QPSGYDNLTF LPDHKAKWSP
710 720 730 740 750
TPNRKPEPSP KLAQPPLRPP SPMSSSPTPP SSTPPSPQPK ASGSPKTVQA
760 770 780 790 800
GDSPSAVRSI LTKERRPEGE GGYKAVWFGK DIGAEADVVV LNEPTADVDS
810 820 830
ASASGSEGSD DDDPDQKKTL RFGVDADNTY I
Length:831
Mass (Da):88,208
Last modified:March 1, 2002 - v1
Checksum:iF0ABF867A37F558B
GO
Isoform 2Curated (identifier: Q8VHF2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     459-620: Missing.

Show »
Length:669
Mass (Da):72,616
Checksum:i15723511BE0D5A22
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti459 – 4602RT → LPSTEF in BAC25662 (PubMed:16141072).Curated
Sequence conflicti621 – 6244Missing in BAC25662 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei459 – 620162Missing in isoform 2. 2 PublicationsVSP_050689Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF462391 mRNA. Translation: AAL67856.1.
AK007988 mRNA. Translation: BAB25392.1.
AK027913 mRNA. Translation: BAC25662.1.
BC054469 mRNA. Translation: AAH54469.1.
CCDSiCCDS22006.1. [Q8VHF2-2]
RefSeqiNP_001107794.1. NM_001114322.1.
NP_082345.1. NM_028069.3. [Q8VHF2-2]
UniGeneiMm.29080.

Genome annotation databases

EnsembliENSMUST00000080654; ENSMUSP00000079484; ENSMUSG00000025497. [Q8VHF2-2]
GeneIDi72040.
KEGGimmu:72040.
UCSCiuc009kkj.2. mouse. [Q8VHF2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF462391 mRNA. Translation: AAL67856.1.
AK007988 mRNA. Translation: BAB25392.1.
AK027913 mRNA. Translation: BAC25662.1.
BC054469 mRNA. Translation: AAH54469.1.
CCDSiCCDS22006.1. [Q8VHF2-2]
RefSeqiNP_001107794.1. NM_001114322.1.
NP_082345.1. NM_028069.3. [Q8VHF2-2]
UniGeneiMm.29080.

3D structure databases

ProteinModelPortaliQ8VHF2.
SMRiQ8VHF2. Positions 70-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000127292.

PTM databases

iPTMnetiQ8VHF2.
PhosphoSiteiQ8VHF2.

Proteomic databases

MaxQBiQ8VHF2.
PaxDbiQ8VHF2.
PRIDEiQ8VHF2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080654; ENSMUSP00000079484; ENSMUSG00000025497. [Q8VHF2-2]
GeneIDi72040.
KEGGimmu:72040.
UCSCiuc009kkj.2. mouse. [Q8VHF2-2]

Organism-specific databases

CTDi53841.
MGIiMGI:1919290. Cdhr5.

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00390000001008.
HOGENOMiHOG000113693.
HOVERGENiHBG052536.
InParanoidiQ8VHF2.
KOiK16505.
PhylomeDBiQ8VHF2.

Miscellaneous databases

NextBioi335280.
PROiQ8VHF2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VHF2.
CleanExiMM_MUPCDH.
ExpressionAtlasiQ8VHF2. baseline and differential.
GenevisibleiQ8VHF2. MM.

Family and domain databases

Gene3Di2.60.40.60. 2 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR030326. Mucdhl.
[Graphical view]
PANTHERiPTHR24027:SF313. PTHR24027:SF313. 1 hit.
SMARTiSM00112. CA. 2 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 2 hits.
PROSITEiPS00232. CADHERIN_1. 1 hit.
PS50268. CADHERIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of mouse mu-protocadherin."
    Soleiman A., Krieger S.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/cJImported.
    Tissue: ColonImported.
  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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Kidney and Pancreas.
  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] (ISOFORM 2).
    Strain: FVB/NImported.
    Tissue: ColonImported.
  4. "mu-protocadherin, a novel developmentally regulated protocadherin with mucin-like domains."
    Goldberg M., Peshkovsky C., Shifteh A., Al-Awqati Q.
    J. Biol. Chem. 275:24622-24629(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-753, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721; SER-725; THR-728; SER-736 AND SER-753, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.

Entry informationi

Entry nameiCDHR5_MOUSE
AccessioniPrimary (citable) accession number: Q8VHF2
Secondary accession number(s): Q8CEJ3, Q9D8I9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 1, 2002
Last modified: May 11, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.