CDHR2_HUMAN
ID CDHR2_HUMAN Reviewed; 1310 AA.
AC Q9BYE9; A1L3U4; A6NC80; Q9NXP8;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cadherin-related family member 2 {ECO:0000305};
DE AltName: Full=Protocadherin LKC {ECO:0000303|PubMed:12117771};
DE Short=PC-LKC {ECO:0000303|PubMed:12117771};
DE AltName: Full=Protocadherin-24 {ECO:0000303|PubMed:24725409};
DE Flags: Precursor;
GN Name=CDHR2 {ECO:0000312|HGNC:HGNC:18231};
GN Synonyms=PCDH24 {ECO:0000303|PubMed:24725409},
GN PCLKC {ECO:0000303|PubMed:12117771};
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB40777.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, TOPOLOGY, INTERACTION WITH MAST2, AND VARIANTS ALA-424 AND
RP MET-1128.
RC TISSUE=Kidney {ECO:0000312|EMBL:BAB40777.1};
RX PubMed=12117771; DOI=10.1093/carcin/23.7.1139;
RA Okazaki N., Takahashi N., Kojima S., Masuho Y., Koga H.;
RT "Protocadherin LKC, a new candidate for a tumor suppressor of colon and
RT liver cancers, its association with contact inhibition of cell
RT proliferation.";
RL Carcinogenesis 23:1139-1148(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA90962.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-424; MET-1128 AND
RP MET-1164.
RC TISSUE=Colon {ECO:0000312|EMBL:BAA90962.1}, and Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-424 AND MET-1128.
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 [5] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=15534908; DOI=10.3748/wjg.v10.i24.3569;
RA Yang L.Y., Wang W., Peng J.X., Yang J.Q., Huang G.W.;
RT "Differentially expressed genes between solitary large hepatocellular
RT carcinoma and nodular hepatocellular carcinoma.";
RL World J. Gastroenterol. 10:3569-3573(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, INTERACTION WITH MYO7B
RP AND USH1C, MUTAGENESIS OF LEU-1310, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1248, AND IDENTIFICATION BY
RP 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 [8]
RP INTERACTION WITH USH1C.
RX PubMed=26812017; DOI=10.1016/j.devcel.2015.12.020;
RA Li J., He Y., Lu Q., Zhang M.;
RT "Mechanistic basis of organization of the Harmonin/USH1C-mediated brush
RT border microvilli tip-link complex.";
RL Dev. Cell 36:179-189(2016).
RN [9]
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).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-1004.
RX PubMed=18987736; DOI=10.1038/nature07485;
RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA DiPersio J.F., Wilson R.K.;
RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT genome.";
RL Nature 456:66-72(2008).
CC -!- FUNCTION: Intermicrovillar adhesion molecule that forms, via its
CC extracellular domain, calcium-dependent heterophilic complexes with
CC CDHR5 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 (PubMed:24725409). May also play a role in cell-cell adhesion and
CC contact inhibition in epithelial cells (PubMed:12117771).
CC {ECO:0000269|PubMed:12117771, 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 with MAST2
CC (PubMed:12117771). Interacts (via cytoplasmic domain) with USH1C and
CC MYO7B; required for proper localization of CDHR2 to microvilli tips and
CC its function in brush border differentiation (PubMed:24725409,
CC PubMed:26812017). {ECO:0000269|PubMed:12117771,
CC ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:26812017,
CC ECO:0000269|PubMed:26812018}.
CC -!- INTERACTION:
CC Q9BYE9; Q9HBB8-1: CDHR5; NbExp=3; IntAct=EBI-493793, EBI-9540729;
CC Q9BYE9; Q9HBB8-2: CDHR5; NbExp=3; IntAct=EBI-493793, EBI-9629917;
CC Q9BYE9; Q6P0Q8: MAST2; NbExp=4; IntAct=EBI-493793, EBI-493777;
CC Q9BYE9; Q6PIF6: MYO7B; NbExp=3; IntAct=EBI-493793, EBI-4400912;
CC Q9BYE9; Q9Y6N9-1: USH1C; NbExp=2; IntAct=EBI-493793, EBI-9541226;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12117771, ECO:0000269|PubMed:24725409}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:12117771,
CC ECO:0000269|PubMed:24725409}. Cell projection, microvillus membrane
CC {ECO:0000269|PubMed:12117771, ECO:0000269|PubMed:24725409}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:12117771,
CC ECO:0000269|PubMed:24725409}. Cell junction
CC {ECO:0000269|PubMed:12117771}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney and colon.
CC Moderately expressed in small intestine. Down-regulated in a number of
CC liver and colon cancers (PubMed:12117771, PubMed:15534908). Expressed
CC in duodenum with higher expression in enterocytes along the villus axis
CC and lower expression in crypts (at protein level) (PubMed:24725409).
CC {ECO:0000269|PubMed:12117771, ECO:0000269|PubMed:15534908,
CC ECO:0000269|PubMed:24725409}.
CC -!- DOMAIN: The cadherin 1 domain is required for binding to CDHR5.
CC {ECO:0000269|PubMed:24725409}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90962.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AB047004; BAB40777.1; -; mRNA.
DR EMBL; AK000131; BAA90962.1; ALT_INIT; mRNA.
DR EMBL; AK315055; BAG37531.1; -; mRNA.
DR EMBL; AC091934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130282; AAI30283.1; -; mRNA.
DR CCDS; CCDS34297.1; -.
DR RefSeq; NP_001165447.1; NM_001171976.1.
DR RefSeq; NP_060145.3; NM_017675.4.
DR PDB; 5CZR; X-ray; 2.30 A; A/B/C/D=21-237.
DR PDB; 7N86; X-ray; 3.17 A; A/B/C/D=21-240.
DR PDBsum; 5CZR; -.
DR PDBsum; 7N86; -.
DR AlphaFoldDB; Q9BYE9; -.
DR SMR; Q9BYE9; -.
DR BioGRID; 120179; 12.
DR IntAct; Q9BYE9; 8.
DR STRING; 9606.ENSP00000424565; -.
DR MoonDB; Q9BYE9; Predicted.
DR GlyConnect; 1922; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9BYE9; 24 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q9BYE9; -.
DR PhosphoSitePlus; Q9BYE9; -.
DR BioMuta; CDHR2; -.
DR DMDM; 209572658; -.
DR jPOST; Q9BYE9; -.
DR MassIVE; Q9BYE9; -.
DR MaxQB; Q9BYE9; -.
DR PaxDb; Q9BYE9; -.
DR PeptideAtlas; Q9BYE9; -.
DR PRIDE; Q9BYE9; -.
DR ProteomicsDB; 79633; -.
DR Antibodypedia; 2236; 41 antibodies from 11 providers.
DR DNASU; 54825; -.
DR Ensembl; ENST00000261944.10; ENSP00000261944.5; ENSG00000074276.11.
DR Ensembl; ENST00000510636.5; ENSP00000424565.1; ENSG00000074276.11.
DR GeneID; 54825; -.
DR KEGG; hsa:54825; -.
DR MANE-Select; ENST00000261944.10; ENSP00000261944.5; NM_017675.6; NP_060145.3.
DR UCSC; uc003mem.3; human.
DR CTD; 54825; -.
DR DisGeNET; 54825; -.
DR GeneCards; CDHR2; -.
DR HGNC; HGNC:18231; CDHR2.
DR HPA; ENSG00000074276; Tissue enriched (intestine).
DR MIM; 619713; gene.
DR neXtProt; NX_Q9BYE9; -.
DR OpenTargets; ENSG00000074276; -.
DR PharmGKB; PA165660231; -.
DR VEuPathDB; HostDB:ENSG00000074276; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000161160; -.
DR HOGENOM; CLU_005755_0_0_1; -.
DR InParanoid; Q9BYE9; -.
DR OMA; TIQAYDN; -.
DR OrthoDB; 83119at2759; -.
DR PhylomeDB; Q9BYE9; -.
DR TreeFam; TF332908; -.
DR PathwayCommons; Q9BYE9; -.
DR SignaLink; Q9BYE9; -.
DR BioGRID-ORCS; 54825; 10 hits in 1065 CRISPR screens.
DR ChiTaRS; CDHR2; human.
DR GeneWiki; PCLKC; -.
DR GenomeRNAi; 54825; -.
DR Pharos; Q9BYE9; Tbio.
DR PRO; PR:Q9BYE9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9BYE9; protein.
DR Bgee; ENSG00000074276; Expressed in jejunal mucosa and 131 other tissues.
DR ExpressionAtlas; Q9BYE9; baseline and differential.
DR Genevisible; Q9BYE9; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IDA:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
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:0060243; P:negative regulation of cell growth involved in contact inhibition; IDA:UniProtKB.
DR GO; GO:0032532; P:regulation of microvillus length; IMP:UniProtKB.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 7.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 9.
DR SUPFAM; SSF49313; SSF49313; 9.
DR PROSITE; PS00232; CADHERIN_1; 7.
DR PROSITE; PS50268; CADHERIN_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Differentiation; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1310
FT /note="Cadherin-related family member 2"
FT /id="PRO_0000004011"
FT TOPO_DOM 21..1154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1155..1175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1176..1310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..124
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 125..241
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 242..353
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 368..480
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 481..586
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 586..695
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 696..808
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 810..928
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 930..1058
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 1180..1310
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 1259..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q7P9"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 775
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 871
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 107
FT /note="Q -> H (in dbSNP:rs6886860)"
FT /id="VAR_046695"
FT VARIANT 415
FT /note="A -> G (in dbSNP:rs3762960)"
FT /id="VAR_046696"
FT VARIANT 424
FT /note="V -> A (in dbSNP:rs11134982)"
FT /evidence="ECO:0000269|PubMed:12117771,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_046697"
FT VARIANT 766
FT /note="L -> P (in dbSNP:rs752138)"
FT /id="VAR_046698"
FT VARIANT 901
FT /note="T -> M (in dbSNP:rs35018750)"
FT /id="VAR_046699"
FT VARIANT 948
FT /note="V -> M (in dbSNP:rs3749625)"
FT /id="VAR_046700"
FT VARIANT 1004
FT /note="P -> L (found in an acute myeloid leukemia sample;
FT somatic mutation; dbSNP:rs371676123)"
FT /evidence="ECO:0000269|PubMed:18987736"
FT /id="VAR_054148"
FT VARIANT 1128
FT /note="T -> M (in dbSNP:rs2291442)"
FT /evidence="ECO:0000269|PubMed:12117771,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_046701"
FT VARIANT 1164
FT /note="L -> M (in dbSNP:rs17078347)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_021548"
FT MUTAGEN 1310
FT /note="L->R: Loss of interaction with USH1C."
FT /evidence="ECO:0000269|PubMed:24725409"
FT CONFLICT 64
FT /note="G -> S (in Ref. 1; BAB40777)"
FT /evidence="ECO:0000305"
FT CONFLICT 1229
FT /note="D -> G (in Ref. 2; BAA90962)"
FT /evidence="ECO:0000305"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5CZR"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5CZR"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5CZR"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:7N86"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5CZR"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5CZR"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:5CZR"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5CZR"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:5CZR"
SQ SEQUENCE 1310 AA; 141543 MW; E0BC8AEEF8D9E1F2 CRC64;
MAQLWLSCFL LPALVVSVAA NVAPKFLANM TSVILPEDLP VGAQAFWLVA EDQDNDPLTY
GMSGPNAYFF AVTPKTGEVK LASALDYETL YTFKVTISVS DPYIQVQREM LVIVEDRNDN
APVFQNTAFS TSINETLPVG SVVFSVLAVD KDMGSAGMVV YSIEKVIPST GDSEHLFRIL
ANGSIVLNGS LSYNNKSAFY QLELKACDLG GMYHNTFTIQ CSLPVFLSIS VVDQPDLDPQ
FVREFYSASV AEDAAKGTSV LTVEAVDGDK GINDPVIYSI SYSTRPGWFD IGADGVIRVN
GSLDREQLLE ADEEVQLQVT ATETHLNIYG QEAKVSIWVT VRVMDVNDHK PEFYNCSLPA
CTFTPEEAQV NFTGYVDEHA SPRIPIDDLT MVVYDPDKGS NGTFLLSLGG PDAEAFSVSP
ERAVGSASVQ VLVRVSALVD YERQTAMAVQ VVATDSVSQN FSVAMVTIHL RDINDHRPTF
PQSLYVLTVP EHSATGSVVT DSIHATDPDT GAWGQITYSL LPGNGADLFQ VDPVSGTVTV
RNGELLDRES QAVYYLTLQA TDGGNLSSST TLQIHLLDIN DNAPVVSGSY NIFVQEEEGN
VSVTIQAHDN DEPGTNNSRL LFNLLPGPYS HNFSLDPDTG LLRNLGPLDR EAIDPALEGR
IVLTVLVSDC GEPVLGTKVN VTITVEDIND NLPIFNQSSY NFTVKEEDPG VLVGVVKAWD
ADQTEANNRI SFSLSGSGAN YFMIRGLVLG AGWAEGYLRL PPDVSLDYET QPVFNLTVSA
ENPDPQGGET IVDVCVNVKD VNDNPPTLDV ASLRGIRVAE NGSQHGQVAV VVASDVDTSA
QLEIQLVNIL CTKAGVDVGS LCWGWFSVAA NGSVYINQSK AIDYEACDLV TLVVRACDLA
TDPGFQAYSN NGSLLITIED VNDNAPYFLP ENKTFVIIPE LVLPNREVAS VRARDDDSGN
NGVILFSILR VDFISKDGAT IPFQGVFSIF TSSEADVFAG SIQPVTSLDS TLQGTYQVTV
QARDRPSLGP FLEATTTLNL FTVDQSYRSR LQFSTPKEEV GANRQAINAA LTQATRTTVY
IVDIQDIDSA ARARPHSYLD AYFVFPNGSA LTLDELSVMI RNDQDSLTQL LQLGLVVLGS
QESQESDLSK QLISVIIGLG VALLLVLVIM TMAFVCVRKS YNRKLQAMKA AKEARKTAAG
VMPSAPAIPG TNMYNTERAN PMLNLPNKDL GLEYLSPSND LDSVSVNSLD DNSVDVDKNS
QEIKEHRPPH TPPEPDPEPL SVVLLGRQAG ASGQLEGPSY TNAGLDTTDL
