CDHR5_MOUSE
ID CDHR5_MOUSE Reviewed; 831 AA.
AC Q8VHF2; Q8CEJ3; Q9D8I9;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cadherin-related family member 5 {ECO:0000305};
DE AltName: Full=Mu-protocadherin {ECO:0000312|EMBL:AAL67856.1};
DE Flags: Precursor;
GN Name=Cdhr5 {ECO:0000312|MGI:MGI:1919290};
GN Synonyms=Mucdhl {ECO:0000312|MGI:MGI:1919290},
GN Mupcdh {ECO:0000312|MGI:MGI:1919290};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAL67856.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAL67856.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAL67856.1};
RA Soleiman A., Krieger S.;
RT "Cloning and characterization of mouse mu-protocadherin.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH54469.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH54469.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=10801787; DOI=10.1074/jbc.m000234200;
RA Goldberg M., Peshkovsky C., Shifteh A., Al-Awqati Q.;
RT "mu-protocadherin, a novel developmentally regulated protocadherin with
RT mucin-like domains.";
RL J. Biol. Chem. 275:24622-24629(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-753, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721; SER-725; THR-728;
RP SER-736 AND SER-753, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Intermicrovillar adhesion molecule that forms, via its
CC extracellular domain, calcium-dependent heterophilic complexes with
CC CDHR2 on adjacent microvilli. Thereby, controls the packing of
CC microvilli at the apical membrane of epithelial cells. Through its
CC cytoplasmic domain, interacts with microvillus cytoplasmic proteins to
CC form the intermicrovillar adhesion complex/IMAC. This complex plays a
CC central role in microvilli and epithelial brush border differentiation.
CC {ECO:0000250|UniProtKB:Q9HBB8}.
CC -!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion
CC complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B,
CC USH1C, CDHR2 and CDHR5. Interacts (via cytoplasmic domain) with USH1C
CC and MYO7B; required for proper localization of CDHR5 to microvilli tips
CC and its function in brush border differentiation.
CC {ECO:0000250|UniProtKB:Q9HBB8}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9HBB8}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9HBB8}. Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:Q9HBB8}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9HBB8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=Q8VHF2-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q8VHF2-2; Sequence=VSP_050689;
CC -!- DEVELOPMENTAL STAGE: Detected at embryonic day 7. Expression decreases
CC by day 11 and increases again between embryonic days 15 and 17.
CC {ECO:0000269|PubMed:10801787}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q9JIK1}.
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DR EMBL; AF462391; AAL67856.1; -; mRNA.
DR EMBL; AK007988; BAB25392.1; -; mRNA.
DR EMBL; AK027913; BAC25662.1; -; mRNA.
DR EMBL; BC054469; AAH54469.1; -; mRNA.
DR CCDS; CCDS22006.1; -. [Q8VHF2-2]
DR RefSeq; NP_001107794.1; NM_001114322.1.
DR RefSeq; NP_082345.1; NM_028069.3. [Q8VHF2-2]
DR AlphaFoldDB; Q8VHF2; -.
DR SMR; Q8VHF2; -.
DR STRING; 10090.ENSMUSP00000127292; -.
DR GlyGen; Q8VHF2; 11 sites.
DR iPTMnet; Q8VHF2; -.
DR PhosphoSitePlus; Q8VHF2; -.
DR jPOST; Q8VHF2; -.
DR MaxQB; Q8VHF2; -.
DR PaxDb; Q8VHF2; -.
DR PRIDE; Q8VHF2; -.
DR ProteomicsDB; 281282; -. [Q8VHF2-1]
DR ProteomicsDB; 281283; -. [Q8VHF2-2]
DR Antibodypedia; 2283; 195 antibodies from 27 providers.
DR DNASU; 72040; -.
DR Ensembl; ENSMUST00000080654; ENSMUSP00000079484; ENSMUSG00000025497. [Q8VHF2-2]
DR GeneID; 72040; -.
DR KEGG; mmu:72040; -.
DR UCSC; uc009kkj.2; mouse. [Q8VHF2-2]
DR CTD; 53841; -.
DR MGI; MGI:1919290; Cdhr5.
DR VEuPathDB; HostDB:ENSMUSG00000025497; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000162463; -.
DR HOGENOM; CLU_021415_0_0_1; -.
DR InParanoid; Q8VHF2; -.
DR OMA; PDYEANT; -.
DR OrthoDB; 1107941at2759; -.
DR PhylomeDB; Q8VHF2; -.
DR BioGRID-ORCS; 72040; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cdhr5; mouse.
DR PRO; PR:Q8VHF2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VHF2; protein.
DR Bgee; ENSMUSG00000025497; Expressed in small intestine Peyer's patch and 54 other tissues.
DR ExpressionAtlas; Q8VHF2; baseline and differential.
DR Genevisible; Q8VHF2; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
DR GO; GO:0044214; C:spanning component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0090675; P:intermicrovillar adhesion; ISS:UniProtKB.
DR GO; GO:0032532; P:regulation of microvillus length; ISS:UniProtKB.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR030326; Mucdhl.
DR PANTHER; PTHR24028:SF243; PTHR24028:SF243; 1.
DR SMART; SM00112; CA; 2.
DR SUPFAM; SSF49313; SSF49313; 2.
DR PROSITE; PS00232; CADHERIN_1; 1.
DR PROSITE; PS50268; CADHERIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection;
KW Differentiation; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..831
FT /note="Cadherin-related family member 5"
FT /id="PRO_0000004013"
FT TOPO_DOM 29..641
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 53..125
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043,
FT ECO:0000305"
FT DOMAIN 128..240
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043,
FT ECO:0000305"
FT DOMAIN 252..357
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043,
FT ECO:0000305"
FT DOMAIN 358..459
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043,
FT ECO:0000305"
FT REPEAT 541..571
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 572..602
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 605..614
FT /note="3; truncated"
FT REGION 452..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..614
FT /note="3 X 31 AA approximate tandem repeats"
FT REGION 663..831
FT /note="Mediates interaction with USH1C and MYO7B and is
FT required for proper localization to microvilli tips and
FT function in microvilli organization"
FT /evidence="ECO:0000250|UniProtKB:Q9HBB8"
FT REGION 675..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..741
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK1"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 728
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 795
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBB8"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBB8"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBB8"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBB8"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT VAR_SEQ 459..620
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_050689"
FT CONFLICT 459..460
FT /note="RT -> LPSTEF (in Ref. 2; BAC25662)"
FT /evidence="ECO:0000305"
FT CONFLICT 621..624
FT /note="Missing (in Ref. 2; BAC25662)"
FT /evidence="ECO:0000305"
SQ 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
