CDHR5_RAT
ID CDHR5_RAT Reviewed; 862 AA.
AC Q9JIK1; Q4FZY9;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cadherin-related family member 5 {ECO:0000305};
DE AltName: Full=GP100 {ECO:0000303|PubMed:10801787};
DE AltName: Full=Mu-protocadherin {ECO:0000303|PubMed:10801787};
DE Flags: Precursor;
GN Name=Cdhr5 {ECO:0000312|RGD:620504};
GN Synonyms=Mucdhl {ECO:0000312|RGD:620504}, Mupcdh {ECO:0000312|RGD:620504};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAF70456.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 132-145;
RP 176-198; 265-280; 416-438 AND 708-722, FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAF70456.1};
RC TISSUE=Kidney {ECO:0000269|PubMed:10801787};
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000305|PubMed:10801787}.
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:0000269|PubMed:10801787};
CC IsoId=Q9JIK1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10801787};
CC IsoId=Q9JIK1-2; Sequence=VSP_050688;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in kidney. Also detected in
CC lung and small intestine. {ECO:0000269|PubMed:10801787}.
CC -!- DEVELOPMENTAL STAGE: At embryonic day 19, both maternal and embryonic
CC kidneys express isoform 1 almost exclusively. In the postpartum female
CC and neonate, expression of isoform 2 increases.
CC {ECO:0000269|PubMed:10801787}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:10801787}.
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DR EMBL; AF221952; AAF70456.1; -; mRNA.
DR EMBL; BC098904; AAH98904.1; -; mRNA.
DR RefSeq; NP_612534.1; NM_138525.1. [Q9JIK1-1]
DR AlphaFoldDB; Q9JIK1; -.
DR SMR; Q9JIK1; -.
DR STRING; 10116.ENSRNOP00000044906; -.
DR GlyGen; Q9JIK1; 9 sites.
DR iPTMnet; Q9JIK1; -.
DR PhosphoSitePlus; Q9JIK1; -.
DR PaxDb; Q9JIK1; -.
DR PRIDE; Q9JIK1; -.
DR Ensembl; ENSRNOT00000044238; ENSRNOP00000044906; ENSRNOG00000017762. [Q9JIK1-1]
DR GeneID; 171554; -.
DR KEGG; rno:171554; -.
DR UCSC; RGD:620504; rat. [Q9JIK1-1]
DR CTD; 53841; -.
DR RGD; 620504; Cdhr5.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000162463; -.
DR HOGENOM; CLU_021415_0_0_1; -.
DR InParanoid; Q9JIK1; -.
DR OMA; PDYEANT; -.
DR OrthoDB; 1107941at2759; -.
DR PhylomeDB; Q9JIK1; -.
DR TreeFam; TF350567; -.
DR PRO; PR:Q9JIK1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017762; Expressed in jejunum and 17 other tissues.
DR Genevisible; Q9JIK1; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
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:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA: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; 3.
DR SUPFAM; SSF49313; SSF49313; 2.
DR PROSITE; PS00232; CADHERIN_1; 1.
DR PROSITE; PS50268; CADHERIN_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection;
KW Differentiation; Direct protein sequencing; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..862
FT /note="Cadherin-related family member 5"
FT /id="PRO_0000004014"
FT TOPO_DOM 29..671
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 693..862
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..127
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..462
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043,
FT ECO:0000305"
FT REPEAT 545..575
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 576..606
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 607..636
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 637..648
FT /note="4; truncated"
FT REGION 452..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..648
FT /note="4 X 31 AA approximate tandem repeats"
FT REGION 693..862
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 706..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..771
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHF2"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHF2"
FT MOD_RES 758
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHF2"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHF2"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHF2"
FT MOD_RES 825
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBB8"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBB8"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBB8"
FT MOD_RES 836
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 135
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 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 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT VAR_SEQ 464..655
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10801787"
FT /id="VSP_050688"
SQ SEQUENCE 862 AA; 90976 MW; 302E302503A9C375 CRC64;
MGAPALLWPP LLLPLLTVLF GHLPGTLAQA QVCSANQTVF TMNENTTVSG PLADIFVPED
QYVTLGQLST PNAFKVEGNK LFLIVTPDYE ENSLLEAVLE CKRGDTLVTQ FRVFVAVLDI
NDNAPEFPFT IKEYNVSEDT RVNTIVIPET ELKATDADKD DILVYTLQEV TPNASKFFSL
VGINSPALKL DQTLDYYKSP NMTFRLLARD TREENVIPSH TATATVVLNV LPADLRTPWF
LPCSFTDDYF CIQAQYHTVI PTGHKLPSPL ILSPGPIYAV DGDQAINQPI VYSIMMGNTD
DTFIINKDDG NLTMAKSIPS PMTFTLVVRA EQADMARYSV TQAVVEARDV TGNPLQFSQS
LYFGTVVLGS EAGTAVKDKT FPSEILRIQA QYLGFPDLNS AVTYQVTNSS EFIMNKDILL
TTVPMETERT IRIEVEANNT VTKDIATTIV EIQVSEREPP STESPTPPEA GGTTGPSSNT
TLETPSTSGT SQGPATTSSG GSAGPFPPAG TTLSPLTSAP TVPGGSPTLG ISTSPQTATP
GGDATQTPKP GTSQPMVPTP GASTSSQPAT PSGSSTQTPK PGTSQPMVPT PGASTSSQPA
TPSGSSTQTP RPGTSQPMVP TPGASTSSQP ATPSGSTQTP KPGTSQPTTT GPISGVGELG
DGQRFSTVDM AVLGGVLGAL LLLALIFLII LIHKHYRHRF TCCSGKAKEP QPSGYDNLTF
LPDNKAKWSP TSNRKPEPGP EPVQPPLRPP SPMSSSPTPP SSMPPSPQPK ASGSPKTVQA
GDSPSAVRSI LTKERRPEGE GGYKAVWFGK DIGAEADVVV LNEPTADVDS ASASGSEGSD
DDDDPDQKKS LRLGAVADNT YV
