CDHR5_HUMAN
ID CDHR5_HUMAN Reviewed; 845 AA.
AC Q9HBB8; C9J7X1; Q9H746; Q9HAU3; Q9HBB5; Q9HBB6; Q9HBB7; Q9NX86; Q9NXI9;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Cadherin-related family member 5 {ECO:0000305};
DE AltName: Full=Mu-protocadherin {ECO:0000312|EMBL:AAG33495.1};
DE AltName: Full=Mucin and cadherin-like protein {ECO:0000303|PubMed:11031102};
DE AltName: Full=Mucin-like protocadherin {ECO:0000303|PubMed:24725409};
DE Short=MLPCDH {ECO:0000303|PubMed:24725409};
DE Flags: Precursor;
GN Name=CDHR5 {ECO:0000312|HGNC:HGNC:7521};
GN Synonyms=MUCDHL {ECO:0000303|PubMed:11031102},
GN MUPCDH {ECO:0000312|HGNC:HGNC:7521};
GN ORFNames=UNQ2781/PRO7168 {ECO:0000312|EMBL:AAQ88734.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAG16731.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS PRO-165;
RP SER-357; SER-521 AND SER-702.
RX PubMed=11031102; DOI=10.1006/geno.2000.6339;
RA Paris M.J., Williams B.R.G.;
RT "Characterization of a 500-kb contig spanning the region between c-Ha-Ras
RT and MUC2 on chromosome 11p15.5.";
RL Genomics 69:196-202(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS SER-357;
RP SER-521 AND SER-702.
RC TISSUE=Kidney {ECO:0000312|EMBL:AAG33495.1};
RA Soleiman A., Krieger S., Haase A., Hantusch B.;
RT "Cloning and characterization of human mu-protocadherin.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS SER-357
RP AND SER-702.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP SER-357; SER-521 AND SER-702.
RC TISSUE=Colon mucosa {ECO:0000312|EMBL:BAA91021.1}, and
RC Ileal mucosa {ECO:0000312|EMBL:BAA91130.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=12167596; DOI=10.1152/ajprenal.00012.2002;
RA Goldberg M., Wei M., Tycko B., Falikovich I., Warburton D.;
RT "Identification and expression analysis of the human mu-protocadherin gene
RT in fetal and adult kidneys.";
RL Am. J. Physiol. 283:F454-F463(2002).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-81 AND ASN-308.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH MYO7B AND USH1C,
RP MUTAGENESIS OF ARG-109 AND ILE-845, REGION, AND TISSUE SPECIFICITY.
RX PubMed=24725409; DOI=10.1016/j.cell.2014.01.067;
RA Crawley S.W., Shifrin D.A. Jr., Grega-Larson N.E., McConnell R.E.,
RA Benesh A.E., Mao S., Zheng Y., Zheng Q.Y., Nam K.T., Millis B.A.,
RA Kachar B., Tyska M.J.;
RT "Intestinal brush border assembly driven by protocadherin-based
RT intermicrovillar adhesion.";
RL Cell 157:433-446(2014).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-810; SER-817; SER-819 AND
RP SER-821, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION OF THE IMAC COMPLEX.
RX PubMed=26812018; DOI=10.1016/j.devcel.2015.12.022;
RA Crawley S.W., Weck M.L., Grega-Larson N.E., Shifrin D.A. Jr., Tyska M.J.;
RT "ANKS4B is essential for intermicrovillar adhesion complex formation.";
RL Dev. Cell 36:190-200(2016).
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:0000269|PubMed:24725409}.
CC -!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion
CC complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B,
CC USH1C, CDHR2 and CDHR5 (PubMed:26812018). Interacts (via cytoplasmic
CC domain) with USH1C and MYO7B; required for proper localization of CDHR5
CC to microvilli tips and its function in brush border differentiation
CC (PubMed:24725409). {ECO:0000269|PubMed:24725409,
CC ECO:0000269|PubMed:26812018}.
CC -!- INTERACTION:
CC Q9HBB8; Q9Y6N9-1: USH1C; NbExp=2; IntAct=EBI-9540696, EBI-9541226;
CC Q9HBB8-1; Q9BYE9: CDHR2; NbExp=3; IntAct=EBI-9540729, EBI-493793;
CC Q9HBB8-2; Q9BYE9: CDHR2; NbExp=3; IntAct=EBI-9629917, EBI-493793;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:24725409}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:24725409}. Cell projection, microvillus membrane
CC {ECO:0000269|PubMed:24725409}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:24725409}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:11031102, ECO:0000305}; Synonyms=MUCDHL-FL
CC {ECO:0000303|PubMed:11031102}, MLPCDH-L {ECO:0000303|PubMed:24725409};
CC IsoId=Q9HBB8-1; Sequence=Displayed;
CC Name=2 {ECO:0000305}; Synonyms=MLPCDH-S {ECO:0000303|PubMed:24725409};
CC IsoId=Q9HBB8-2; Sequence=VSP_050693;
CC Name=3;
CC IsoId=Q9HBB8-4; Sequence=VSP_050692;
CC -!- TISSUE SPECIFICITY: Highest expression in kidney, liver, colon and
CC small intestine. In kidney, expressed apically along brush border of
CC proximal convoluted tubule but not in cortical collecting ducts.
CC Isoform 1 is expressed primarily in adult small intestine and colon.
CC Isoform 2 is highly expressed in fetal liver (PubMed:12167596).
CC Expressed in duodenum with higher expression in enterocytes along the
CC villus axis and lower expression in crypts (at protein level)
CC (PubMed:24725409). {ECO:0000269|PubMed:12167596,
CC ECO:0000269|PubMed:24725409}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q9JIK1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG16730.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG16732.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAA91021.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91021.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91021.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAB15052.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A tighter mesh - Issue 178
CC of April 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/178/";
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DR EMBL; AF258674; AAG16730.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF258674; AAG16731.1; -; Genomic_DNA.
DR EMBL; AF258675; AAG16732.1; ALT_SEQ; mRNA.
DR EMBL; AF258676; AAG16733.1; -; mRNA.
DR EMBL; AF276242; AAG30821.1; -; mRNA.
DR EMBL; AF301909; AAG33495.1; -; mRNA.
DR EMBL; AY358368; AAQ88734.1; -; mRNA.
DR EMBL; AK000226; BAA91021.1; ALT_SEQ; mRNA.
DR EMBL; AK000384; BAA91130.1; -; mRNA.
DR EMBL; AK025012; BAB15052.1; ALT_FRAME; mRNA.
DR EMBL; AP006284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS7707.1; -. [Q9HBB8-1]
DR CCDS; CCDS7708.1; -. [Q9HBB8-2]
DR RefSeq; NP_001165439.1; NM_001171968.1. [Q9HBB8-4]
DR RefSeq; NP_068743.2; NM_021924.4. [Q9HBB8-1]
DR RefSeq; NP_112554.2; NM_031264.3. [Q9HBB8-2]
DR PDB; 6OAE; X-ray; 1.90 A; A=26-232.
DR PDBsum; 6OAE; -.
DR AlphaFoldDB; Q9HBB8; -.
DR SMR; Q9HBB8; -.
DR BioGRID; 119810; 25.
DR IntAct; Q9HBB8; 13.
DR STRING; 9606.ENSP00000351118; -.
DR GlyConnect; 1923; 4 N-Linked glycans (3 sites).
DR GlyGen; Q9HBB8; 11 sites, 4 N-linked glycans (3 sites), 2 O-linked glycans (3 sites).
DR iPTMnet; Q9HBB8; -.
DR PhosphoSitePlus; Q9HBB8; -.
DR BioMuta; CDHR5; -.
DR DMDM; 296439399; -.
DR jPOST; Q9HBB8; -.
DR MassIVE; Q9HBB8; -.
DR MaxQB; Q9HBB8; -.
DR PaxDb; Q9HBB8; -.
DR PeptideAtlas; Q9HBB8; -.
DR PRIDE; Q9HBB8; -.
DR ProteomicsDB; 81519; -. [Q9HBB8-1]
DR ProteomicsDB; 81520; -. [Q9HBB8-2]
DR ProteomicsDB; 81521; -. [Q9HBB8-4]
DR Antibodypedia; 2283; 195 antibodies from 27 providers.
DR DNASU; 53841; -.
DR Ensembl; ENST00000349570.11; ENSP00000345726.7; ENSG00000099834.19. [Q9HBB8-2]
DR Ensembl; ENST00000358353.8; ENSP00000351118.4; ENSG00000099834.19. [Q9HBB8-4]
DR Ensembl; ENST00000397542.7; ENSP00000380676.2; ENSG00000099834.19. [Q9HBB8-1]
DR Ensembl; ENST00000674088.1; ENSP00000501074.1; ENSG00000099834.19. [Q9HBB8-1]
DR GeneID; 53841; -.
DR KEGG; hsa:53841; -.
DR MANE-Select; ENST00000397542.7; ENSP00000380676.2; NM_021924.5; NP_068743.3.
DR UCSC; uc001lqj.3; human. [Q9HBB8-1]
DR CTD; 53841; -.
DR DisGeNET; 53841; -.
DR GeneCards; CDHR5; -.
DR HGNC; HGNC:7521; CDHR5.
DR HPA; ENSG00000099834; Group enriched (intestine, liver).
DR MIM; 606839; gene.
DR neXtProt; NX_Q9HBB8; -.
DR OpenTargets; ENSG00000099834; -.
DR PharmGKB; PA165543311; -.
DR VEuPathDB; HostDB:ENSG00000099834; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000162463; -.
DR InParanoid; Q9HBB8; -.
DR OMA; PDYEANT; -.
DR OrthoDB; 1107941at2759; -.
DR PhylomeDB; Q9HBB8; -.
DR TreeFam; TF350567; -.
DR PathwayCommons; Q9HBB8; -.
DR SignaLink; Q9HBB8; -.
DR BioGRID-ORCS; 53841; 8 hits in 1060 CRISPR screens.
DR ChiTaRS; CDHR5; human.
DR GeneWiki; MUPCDH; -.
DR GenomeRNAi; 53841; -.
DR Pharos; Q9HBB8; Tbio.
DR PRO; PR:Q9HBB8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9HBB8; protein.
DR Bgee; ENSG00000099834; Expressed in duodenum and 101 other tissues.
DR ExpressionAtlas; Q9HBB8; baseline and differential.
DR Genevisible; Q9HBB8; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA: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; IMP:UniProtKB.
DR GO; GO:0032532; P:regulation of microvillus length; IMP: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; 2.
DR SMART; SM00112; CA; 3.
DR SUPFAM; SSF49313; SSF49313; 3.
DR PROSITE; PS00232; CADHERIN_1; 1.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane;
KW Cell projection; Differentiation; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..845
FT /note="Cadherin-related family member 5"
FT /id="PRO_0000004012"
FT TOPO_DOM 26..669
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 670..690
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 691..845
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 71..124
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043,
FT ECO:0000305"
FT DOMAIN 125..237
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043,
FT ECO:0000305"
FT DOMAIN 249..354
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043,
FT ECO:0000305"
FT DOMAIN 355..459
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043,
FT ECO:0000305"
FT REPEAT 540..570
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 571..601
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 602..631
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 632..645
FT /note="4; truncated"
FT REGION 452..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..645
FT /note="4 X 31 AA approximate tandem repeats"
FT REGION 691..845
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:0000269|PubMed:24725409"
FT REGION 724..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHF2"
FT MOD_RES 810
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT VAR_SEQ 460..653
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_050693"
FT VAR_SEQ 460..465
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_050692"
FT VARIANT 165
FT /note="Q -> P (in dbSNP:rs2740374)"
FT /evidence="ECO:0000269|PubMed:11031102"
FT /id="VAR_060412"
FT VARIANT 357
FT /note="R -> S (in dbSNP:rs2246614)"
FT /evidence="ECO:0000269|PubMed:11031102,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039,
FT ECO:0000269|Ref.2"
FT /id="VAR_017920"
FT VARIANT 389
FT /note="D -> N (in dbSNP:rs2306066)"
FT /id="VAR_017921"
FT VARIANT 521
FT /note="P -> S (in dbSNP:rs2740375)"
FT /evidence="ECO:0000269|PubMed:11031102,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_060413"
FT VARIANT 702
FT /note="C -> S (in dbSNP:rs2740379)"
FT /evidence="ECO:0000269|PubMed:11031102,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039,
FT ECO:0000269|Ref.2"
FT /id="VAR_059192"
FT MUTAGEN 109
FT /note="R->G: Loss of binding to CDHR2."
FT /evidence="ECO:0000269|PubMed:24725409"
FT MUTAGEN 845
FT /note="I->R: Loss of interaction with USH1C."
FT /evidence="ECO:0000269|PubMed:24725409"
FT CONFLICT 313
FT /note="R -> S (in Ref. 4; BAA91021)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="V -> A (in Ref. 4; BAB15052)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="S -> G (in Ref. 2; AAG33495 and 4; BAA91021)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="G -> E (in Ref. 2; AAG33495 and 4; BAA91021)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="A -> V (in Ref. 1; AAG16733, 2; AAG33495 and 4;
FT BAA91021)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="N -> S (in Ref. 2; AAG30821/AAG33495 and 4;
FT BAA91130)"
FT /evidence="ECO:0000305"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:6OAE"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6OAE"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 103..115
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6OAE"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:6OAE"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6OAE"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 197..209
FT /evidence="ECO:0007829|PDB:6OAE"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:6OAE"
SQ SEQUENCE 845 AA; 88223 MW; FD872A8D67AF6677 CRC64;
MGSWALLWPP LLFTGLLVRP PGTMAQAQYC SVNKDIFEVE ENTNVTEPLV DIHVPEGQEV
TLGALSTPFA FRIQGNQLFL NVTPDYEEKS LLEAQLLCQS GGTLVTQLRV FVSVLDVNDN
APEFPFKTKE IRVEEDTKVN STVIPETQLQ AEDRDKDDIL FYTLQEMTAG ASDYFSLVSV
NRPALRLDRP LDFYERPNMT FWLLVRDTPG ENVEPSHTAT ATLVLNVVPA DLRPPWFLPC
TFSDGYVCIQ AQYHGAVPTG HILPSPLVLR PGPIYAEDGD RGINQPIIYS IFRGNVNGTF
IIHPDSGNLT VARSVPSPMT FLLLVKGQQA DLARYSVTQV TVEAVAAAGS PPRFPQRLYR
GTVARGAGAG VVVKDAAAPS QPLRIQAQDP EFSDLNSAIT YRITNHSHFR MEGEVVLTTT
TLAQAGAFYA EVEAHNTVTS GTATTVIEIQ VSEQEPPSTD VPPSPEAGGT TGPWTSTTSE
VPRPPEPSQG PSTTSSGGGT GPHPPSGTTL RPPTSSTPGG PPGAENSTSH QPATPGGDTA
QTPKPGTSQP MPPGVGTSTS HQPATPSGGT AQTPEPGTSQ PMPPSMGTST SHQPATPGGG
TAQTPEAGTS QPMPPGMGTS TSHQPTTPGG GTAQTPEPGT SQPMPLSKST PSSGGGPSED
KRFSVVDMAA LGGVLGALLL LALLGLAVLV HKHYGPRLKC CCGKAPEPQP QGFDNQAFLP
DHKANWAPVP SPTHDPKPAE APMPAEPAPP GPASPGGAPE PPAAARAGGS PTAVRSILTK
ERRPEGGYKA VWFGEDIGTE ADVVVLNAPT LDVDGASDSG SGDEGEGAGR GGGPYDAPGG
DDSYI
