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Cadherin-related family member 5 (Mu-protocadherin)

 CDHR5_MOUSE             Reviewed;         831 AA.
Q8VHF2; Q8CEJ3; Q9D8I9;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
20-JUN-2018, entry version 123.
RecName: Full=Cadherin-related family member 5 {ECO:0000305};
AltName: Full=Mu-protocadherin {ECO:0000312|EMBL:AAL67856.1};
Flags: Precursor;
Name=Cdhr5 {ECO:0000312|MGI:MGI:1919290};
Synonyms=Mucdhl {ECO:0000312|MGI:MGI:1919290},
Mupcdh {ECO:0000312|MGI:MGI:1919290};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAL67856.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ {ECO:0000312|EMBL:AAL67856.1};
TISSUE=Colon {ECO:0000312|EMBL:AAL67856.1};
Soleiman A., Krieger S.;
"Cloning and characterization of mouse mu-protocadherin.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Kidney, and Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N {ECO:0000312|EMBL:AAH54469.1};
TISSUE=Colon {ECO:0000312|EMBL:AAH54469.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000305}
DEVELOPMENTAL STAGE.
PubMed=10801787; DOI=10.1074/jbc.M000234200;
Goldberg M., Peshkovsky C., Shifteh A., Al-Awqati Q.;
"mu-protocadherin, a novel developmentally regulated protocadherin
with mucin-like domains.";
J. Biol. Chem. 275:24622-24629(2000).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-753, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721; SER-725; THR-728;
SER-736 AND SER-753, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:Q9HBB8}.
-!- SUBUNIT: 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.
{ECO:0000250|UniProtKB:Q9HBB8}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000250|UniProtKB:Q9HBB8}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q9HBB8}. Cell projection,
microvillus membrane {ECO:0000250|UniProtKB:Q9HBB8}; Single-pass
type I membrane protein {ECO:0000250|UniProtKB:Q9HBB8}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000305};
IsoId=Q8VHF2-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q8VHF2-2; Sequence=VSP_050689;
-!- DEVELOPMENTAL STAGE: Detected at embryonic day 7. Expression
decreases by day 11 and increases again between embryonic days 15
and 17. {ECO:0000269|PubMed:10801787}.
-!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q9JIK1}.
-----------------------------------------------------------------------
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EMBL; AF462391; AAL67856.1; -; mRNA.
EMBL; AK007988; BAB25392.1; -; mRNA.
EMBL; AK027913; BAC25662.1; -; mRNA.
EMBL; BC054469; AAH54469.1; -; mRNA.
CCDS; CCDS22006.1; -. [Q8VHF2-2]
RefSeq; NP_001107794.1; NM_001114322.1.
RefSeq; NP_082345.1; NM_028069.3. [Q8VHF2-2]
UniGene; Mm.29080; -.
ProteinModelPortal; Q8VHF2; -.
STRING; 10090.ENSMUSP00000127292; -.
iPTMnet; Q8VHF2; -.
PhosphoSitePlus; Q8VHF2; -.
PaxDb; Q8VHF2; -.
PRIDE; Q8VHF2; -.
Ensembl; ENSMUST00000080654; ENSMUSP00000079484; ENSMUSG00000025497. [Q8VHF2-2]
GeneID; 72040; -.
KEGG; mmu:72040; -.
UCSC; uc009kkj.2; mouse. [Q8VHF2-2]
CTD; 53841; -.
MGI; MGI:1919290; Cdhr5.
eggNOG; KOG3594; Eukaryota.
eggNOG; ENOG410XQHI; LUCA.
GeneTree; ENSGT00390000001008; -.
HOGENOM; HOG000113693; -.
HOVERGEN; HBG052536; -.
InParanoid; Q8VHF2; -.
KO; K16505; -.
PhylomeDB; Q8VHF2; -.
PRO; PR:Q8VHF2; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000025497; -.
CleanEx; MM_MUPCDH; -.
ExpressionAtlas; Q8VHF2; baseline and differential.
Genevisible; Q8VHF2; MM.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
GO; GO:0044214; C:spanning component of plasma membrane; ISS:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0090675; P:intermicrovillar adhesion; ISS:UniProtKB.
GO; GO:0032532; P:regulation of microvillus length; ISS:UniProtKB.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR030326; Mucdhl.
PANTHER; PTHR45160; PTHR45160; 1.
SMART; SM00112; CA; 2.
SUPFAM; SSF49313; SSF49313; 2.
PROSITE; PS00232; CADHERIN_1; 1.
PROSITE; PS50268; CADHERIN_2; 2.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell membrane; Cell projection;
Complete proteome; Differentiation; Glycoprotein; Membrane;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 831 Cadherin-related family member 5.
/FTId=PRO_0000004013.
TOPO_DOM 29 641 Extracellular. {ECO:0000255}.
TRANSMEM 642 662 Helical. {ECO:0000255}.
TOPO_DOM 663 831 Cytoplasmic. {ECO:0000255}.
DOMAIN 53 125 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043, ECO:0000305}.
DOMAIN 128 240 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043, ECO:0000305}.
DOMAIN 252 357 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043, ECO:0000305}.
DOMAIN 358 459 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043, ECO:0000305}.
REPEAT 541 571 1. {ECO:0000305}.
REPEAT 572 602 2. {ECO:0000305}.
REPEAT 605 614 3; truncated.
REGION 541 614 3 X 31 AA approximate tandem repeats.
REGION 663 831 Mediates interaction with USH1C and MYO7B
and is required for proper localization
to microvilli tips and function in
microvilli organization.
{ECO:0000250|UniProtKB:Q9HBB8}.
MOD_RES 699 699 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JIK1}.
MOD_RES 721 721 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 725 725 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 728 728 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 753 753 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 795 795 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9HBB8}.
MOD_RES 802 802 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HBB8}.
MOD_RES 804 804 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HBB8}.
MOD_RES 806 806 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HBB8}.
CARBOHYD 36 36 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 475 475 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
VAR_SEQ 459 620 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_050689.
CONFLICT 459 460 RT -> LPSTEF (in Ref. 2; BAC25662).
{ECO:0000305}.
CONFLICT 621 624 Missing (in Ref. 2; BAC25662).
{ECO:0000305}.
SEQUENCE 831 AA; 88208 MW; F0ABF867A37F558B CRC64;
MGAPALLWPS LLLPWLTVLF GQPPGTLAQT QVCSVNQTIF RVEENTTVSE PLVNIFVPDG
LHVTLGPLST PYAFRIEGKD LFLNVTPDYE ENSLLQADVE CKRGDAVVVR LEVFVAVLDI
NDNAPKFSFE IKTFNVSEDT KVNTTVIPET QLKATDADIN DILVYTLQEV TPNASKFFSL
EGVNYPALKL DQTLDYFKNQ NMTFMLLARD TWEENVEPSH TATATLVLNT LPADLRTPWF
LPCSFTDGYV CIHAQYSAVV PTGHKLPSPL IMSPGPIYAV DGDQAINQSI IYSIIAGNTD
GTFIINAHDG NLTMTKSIPS PMKFTLLIRA DQEDMAQYSV TQAIVEARSV TGNPLQFSQS
LYYGTVVLGS EAGTAVKDKT FPSEILRIQA QYPGFPDLNS AVTYRVTNSS EFMMNKDIML
TAVPMEEART IRVEVEASNT VTKDTATAVV EIQVSERERT PTPPEAGGTT GPSSNTTMEA
PLTSGTSQRP ATTSSGGSVG PFPPGGTTLR PPTPASSIPG GSPTLGTSTS PQTTTPGGDS
AQTPKPGTSH PTAPTSRTST SLMTTSSRSD STQTPKPGTS QPMVPIPGAS TSSQPATPSG
SSPQTPKPGT SQSTATGPIS LPSTGAGEQG DGQRFSTVDM AVLGGVLGAL LLLALICLVI
LVHKHYRHRL ACCSGKASEP QPSGYDNLTF LPDHKAKWSP TPNRKPEPSP KLAQPPLRPP
SPMSSSPTPP SSTPPSPQPK ASGSPKTVQA GDSPSAVRSI LTKERRPEGE GGYKAVWFGK
DIGAEADVVV LNEPTADVDS ASASGSEGSD DDDPDQKKTL RFGVDADNTY I


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