ID DJC13_HUMAN Reviewed; 2243 AA. AC O75165; Q3L0T1; Q6PI82; Q6UJ77; Q6ZSW1; Q6ZUT5; Q86XG3; Q96DC1; Q9BWK9; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 5. DT 27-MAR-2024, entry version 185. DE RecName: Full=DnaJ homolog subfamily C member 13; DE AltName: Full=Required for receptor-mediated endocytosis 8; DE Short=RME-8; GN Name=DNAJC13; Synonyms=KIAA0678, RME8; 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] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=16179350; DOI=10.1074/jbc.m505036200; RA Girard M., Poupon V., Blondeau F., McPherson P.S.; RT "The DnaJ-domain protein RME-8 functions in endosomal trafficking."; RL J. Biol. Chem. 280:40135-40143(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-1463. RC TISSUE=Brain; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [3] RP SEQUENCE REVISION. RC TISSUE=Aortic endothelium; RA Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-736 AND 1819-2243. RC TISSUE=Cervix, Placenta, and Uterus; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 617-2243, AND VARIANT SER-1463. RC TISSUE=Brain; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 672-1098. RA Chang H.C., Hull M.J., Mellman I.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18256511; DOI=10.1247/csf.07045; RA Fujibayashi A., Taguchi T., Misaki R., Ohtani M., Dohmae N., Takio K., RA Yamada M., Gu J., Yamakami M., Fukuda M., Waguri S., Uchiyama Y., RA Yoshimori T., Sekiguchi K.; RT "Human RME-8 is involved in membrane trafficking through early endosomes."; RL Cell Struct. Funct. 33:35-50(2008). RN [9] RP FUNCTION. RX PubMed=18307993; DOI=10.1016/j.febslet.2008.02.042; RA Girard M., McPherson P.S.; RT "RME-8 regulates trafficking of the epidermal growth factor receptor."; RL FEBS Lett. 582:961-966(2008). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP POSSIBLE INVOLVEMENT IN PARK, VARIANT PARK SER-855, VARIANTS GLN-264; RP ILE-1082 AND LEU-2115, AND CHARACTERIZATION OF VARIANT PARK SER-855. RX PubMed=24218364; DOI=10.1093/hmg/ddt570; RA Vilarino-Guell C., Rajput A., Milnerwood A.J., Shah B., Szu-Tu C., RA Trinh J., Yu I., Encarnacion M., Munsie L.N., Tapia L., Gustavsson E.K., RA Chou P., Tatarnikov I., Evans D.M., Pishotta F.T., Volta M., RA Beccano-Kelly D., Thompson C., Lin M.K., Sherman H.E., Han H.J., RA Guenther B.L., Wasserman W.W., Bernard V., Ross C.J., Appel-Cresswell S., RA Stoessl A.J., Robinson C.A., Dickson D.W., Ross O.A., Wszolek Z.K., RA Aasly J.O., Wu R.M., Hentati F., Gibson R.A., McPherson P.S., Girard M., RA Rajput M., Rajput A.H., Farrer M.J.; RT "DNAJC13 mutations in Parkinson disease."; RL Hum. Mol. Genet. 23:1794-1801(2014). RN [13] RP FUNCTION, INTERACTION WITH WASHC2C, AND SUBCELLULAR LOCATION. RX PubMed=24643499; DOI=10.1242/jcs.144659; RA Freeman C.L., Hesketh G., Seaman M.N.; RT "RME-8 coordinates the activity of the WASH complex with the function of RT the retromer SNX dimer to control endosomal tubulation."; RL J. Cell Sci. 127:2053-2070(2014). RN [14] RP POSSIBLE INVOLVEMENT IN PARK, VARIANTS SER-556; ALA-674; LYS-903; PHE-997; RP SER-1135; GLY-1291; HIS-1516; GLN-1740; SER-2057 AND TRP-2170, AND VARIANTS RP PARK LEU-722; SER-855; GLN-1266 AND MET-1895. RX PubMed=25393719; DOI=10.1002/mds.26064; RA Gustavsson E.K., Trinh J., Guella I., Vilarino-Gueell C., RA Appel-Cresswell S., Stoessl A.J., Tsui J.K., McKeown M., Rajput A., RA Rajput A.H., Aasly J.O., Farrer M.J.; RT "DNAJC13 genetic variants in parkinsonism."; RL Mov. Disord. 30:273-278(2015). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [16] RP DISCUSSION ON POSSIBLE INVOLVEMENT IN PARK. RX PubMed=27270108; DOI=10.1038/ng.3589; RA Deng H.X., Shi Y., Yang Y., Ahmeti K.B., Miller N., Huang C., Cheng L., RA Zhai H., Deng S., Nuytemans K., Corbett N.J., Kim M.J., Deng H., Tang B., RA Yang Z., Xu Y., Chan P., Huang B., Gao X.P., Song Z., Liu Z., Fecto F., RA Siddique N., Foroud T., Jankovic J., Ghetti B., Nicholson D.A., Krainc D., RA Melen O., Vance J.M., Pericak-Vance M.A., Ma Y.C., Rajput A.H., RA Siddique T.; RT "Identification of TMEM230 mutations in familial Parkinson's disease."; RL Nat. Genet. 48:733-739(2016). CC -!- FUNCTION: Involved in membrane trafficking through early endosomes, CC such as the early endosome to recycling endosome transport implicated CC in the recycling of transferrin and the early endosome to late endosome CC transport implicated in degradation of EGF and EGFR (PubMed:18256511, CC PubMed:18307993). Involved in the regulation of endosomal membrane CC tubulation and regulates the dynamics of SNX1 on the endosomal CC membrane; via association with WASHC2 may link the WASH complex to the CC retromer SNX-BAR subcomplex (PubMed:24643499). CC {ECO:0000269|PubMed:18256511, ECO:0000269|PubMed:18307993, CC ECO:0000269|PubMed:24643499}. CC -!- SUBUNIT: Interacts with WASHC2C; mediates the association with the WASH CC complex (PubMed:24643499). {ECO:0000269|PubMed:24643499}. CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:18256511}. CC Early endosome membrane {ECO:0000305}; Peripheral membrane protein CC {ECO:0000269|PubMed:18256511}. Endosome membrane CC {ECO:0000269|PubMed:24643499}. CC -!- DISEASE: Parkinson disease (PARK) [MIM:168600]: A complex CC neurodegenerative disorder characterized by bradykinesia, resting CC tremor, muscular rigidity and postural instability. Additional features CC are characteristic postural abnormalities, dysautonomia, dystonic CC cramps, and dementia. The pathology of Parkinson disease involves the CC loss of dopaminergic neurons in the substantia nigra and the presence CC of Lewy bodies (intraneuronal accumulations of aggregated proteins), in CC surviving neurons in various areas of the brain. The disease is CC progressive and usually manifests after the age of 50 years, although CC early-onset cases (before 50 years) are known. The majority of the CC cases are sporadic suggesting a multifactorial etiology based on CC environmental and genetic factors. However, some patients present with CC a positive family history for the disease. Familial forms of the CC disease usually begin at earlier ages and are associated with atypical CC clinical features. {ECO:0000269|PubMed:24218364, CC ECO:0000269|PubMed:25393719}. Note=The gene represented in this entry CC may be involved in disease pathogenesis. Genetic variants in DNAJC13 CC (PubMed:24218364, PubMed:25393719) and TMEM230 (PubMed:27270108) have CC been found in the same large multigenerational family with adult-onset CC Parkinson disease. The pathological role of each gene and therefore the CC exact molecular basis of the disease is unclear. CC {ECO:0000305|PubMed:27270108}. CC -!- CAUTION: In human, WASHC2 has undergone evolutionary duplication giving CC rise to highly homologous family members. A WASHC2C construct with CC WASHC2A-specific sequence insertions (of 2 aa and 21 aa length CC resulting in a construct length of 1341 aa similar to WASHC2A length) CC has been used to demonstrate the interaction with WASHC2 CC (PubMed:24643499). {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH43583.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC Sequence=BAA31653.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC86133.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC86835.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC86835.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY779857; AAV41096.1; -; mRNA. DR EMBL; AB014578; BAA31653.2; ALT_INIT; mRNA. DR EMBL; AC020632; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC020633; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026374; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000164; AAH00164.2; -; mRNA. DR EMBL; BC009630; AAH09630.1; -; mRNA. DR EMBL; BC040638; AAH40638.1; -; mRNA. DR EMBL; BC043583; AAH43583.1; ALT_SEQ; mRNA. DR EMBL; AK125330; BAC86133.1; ALT_INIT; mRNA. DR EMBL; AK127112; BAC86835.1; ALT_SEQ; mRNA. DR EMBL; AY369172; AAQ57271.1; -; mRNA. DR CCDS; CCDS33857.1; -. DR PIR; T00361; T00361. DR RefSeq; NP_056083.3; NM_015268.3. DR AlphaFoldDB; O75165; -. DR SMR; O75165; -. DR BioGRID; 116908; 147. DR IntAct; O75165; 51. DR MINT; O75165; -. DR STRING; 9606.ENSP00000260818; -. DR GlyGen; O75165; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O75165; -. DR MetOSite; O75165; -. DR PhosphoSitePlus; O75165; -. DR SwissPalm; O75165; -. DR BioMuta; DNAJC13; -. DR EPD; O75165; -. DR jPOST; O75165; -. DR MassIVE; O75165; -. DR MaxQB; O75165; -. DR PaxDb; 9606-ENSP00000260818; -. DR PeptideAtlas; O75165; -. DR ProteomicsDB; 49830; -. DR Pumba; O75165; -. DR Antibodypedia; 51566; 60 antibodies from 20 providers. DR Ensembl; ENST00000260818.11; ENSP00000260818.6; ENSG00000138246.17. DR GeneID; 23317; -. DR KEGG; hsa:23317; -. DR MANE-Select; ENST00000260818.11; ENSP00000260818.6; NM_015268.4; NP_056083.3. DR UCSC; uc003eor.4; human. DR AGR; HGNC:30343; -. DR CTD; 23317; -. DR DisGeNET; 23317; -. DR GeneCards; DNAJC13; -. DR HGNC; HGNC:30343; DNAJC13. DR HPA; ENSG00000138246; Low tissue specificity. DR MalaCards; DNAJC13; -. DR MIM; 168600; phenotype. DR MIM; 614334; gene. DR neXtProt; NX_O75165; -. DR OpenTargets; ENSG00000138246; -. DR Orphanet; 411602; Hereditary late-onset Parkinson disease. DR PharmGKB; PA134947358; -. DR VEuPathDB; HostDB:ENSG00000138246; -. DR eggNOG; KOG1789; Eukaryota. DR GeneTree; ENSGT00390000017582; -. DR HOGENOM; CLU_001238_1_0_1; -. DR InParanoid; O75165; -. DR OMA; ELRPYKY; -. DR OrthoDB; 69840at2759; -. DR PhylomeDB; O75165; -. DR TreeFam; TF105172; -. DR PathwayCommons; O75165; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; O75165; -. DR BioGRID-ORCS; 23317; 78 hits in 1161 CRISPR screens. DR ChiTaRS; DNAJC13; human. DR GeneWiki; DNAJC13; -. DR GenomeRNAi; 23317; -. DR Pharos; O75165; Tbio. DR PRO; PR:O75165; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O75165; Protein. DR Bgee; ENSG00000138246; Expressed in calcaneal tendon and 209 other cell types or tissues. DR ExpressionAtlas; O75165; baseline and differential. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB. DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central. DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; IMP:UniProtKB. DR GO; GO:1902954; P:regulation of early endosome to recycling endosome transport; IMP:UniProtKB. DR CDD; cd06257; DnaJ; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR044978; GRV2/DNAJC13. DR InterPro; IPR045802; GRV2/DNAJC13_N. DR InterPro; IPR035445; GYF-like_dom_sf. DR InterPro; IPR025640; GYF_2. DR InterPro; IPR036869; J_dom_sf. DR PANTHER; PTHR36983; DNAJ HOMOLOG SUBFAMILY C MEMBER 13; 1. DR PANTHER; PTHR36983:SF2; DNAJ HOMOLOG SUBFAMILY C MEMBER 13; 1. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF14237; GYF_2; 1. DR Pfam; PF19432; RME-8_N; 1. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF48371; ARM repeat; 3. DR SUPFAM; SSF46565; Chaperone J-domain; 1. DR SUPFAM; SSF55277; GYF domain; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR Genevisible; O75165; HS. PE 1: Evidence at protein level; KW Acetylation; Chaperone; Disease variant; Endosome; Membrane; KW Neurodegeneration; Parkinson disease; Parkinsonism; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..2243 FT /note="DnaJ homolog subfamily C member 13" FT /id="PRO_0000071072" FT DOMAIN 1301..1366 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT REGION 1..453 FT /note="Involved in membrane association" FT /evidence="ECO:0000269|PubMed:18256511" FT MOD_RES 84 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 264 FT /note="E -> Q" FT /evidence="ECO:0000269|PubMed:24218364" FT /id="VAR_073784" FT VARIANT 556 FT /note="L -> S (in dbSNP:rs749000301)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076716" FT VARIANT 674 FT /note="D -> A (in dbSNP:rs199541720)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076717" FT VARIANT 722 FT /note="V -> L (in PARK; uncertain significance; FT dbSNP:rs146930051)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076718" FT VARIANT 855 FT /note="N -> S (in PARK; uncertain significance; affects FT regulation of endosomal membrane trafficking as indicated FT by accumulation of transferrin in endosomal compartments; FT dbSNP:rs387907571)" FT /evidence="ECO:0000269|PubMed:24218364, FT ECO:0000269|PubMed:25393719" FT /id="VAR_073785" FT VARIANT 903 FT /note="R -> K (in dbSNP:rs141952333)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076719" FT VARIANT 997 FT /note="L -> F (in dbSNP:rs752189478)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076720" FT VARIANT 1082 FT /note="T -> I (in dbSNP:rs202127368)" FT /evidence="ECO:0000269|PubMed:24218364" FT /id="VAR_073786" FT VARIANT 1135 FT /note="N -> S (in dbSNP:rs751747947)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076721" FT VARIANT 1266 FT /note="R -> Q (in PARK; uncertain significance; FT dbSNP:rs766013346)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076722" FT VARIANT 1291 FT /note="E -> G (in dbSNP:rs61748101)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076723" FT VARIANT 1463 FT /note="A -> S (in dbSNP:rs3762672)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9734811" FT /id="VAR_047458" FT VARIANT 1487 FT /note="F -> C (in dbSNP:rs4405917)" FT /id="VAR_047459" FT VARIANT 1515 FT /note="P -> S (in dbSNP:rs55825559)" FT /id="VAR_061144" FT VARIANT 1516 FT /note="R -> H (in dbSNP:rs139620588)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076724" FT VARIANT 1740 FT /note="E -> Q (in dbSNP:rs142160751)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076725" FT VARIANT 1895 FT /note="T -> M (in PARK; uncertain significance; FT dbSNP:rs145242123)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076726" FT VARIANT 1995 FT /note="V -> I (in dbSNP:rs10935014)" FT /id="VAR_047460" FT VARIANT 2057 FT /note="A -> S (in dbSNP:rs138693725)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076727" FT VARIANT 2115 FT /note="R -> L (in dbSNP:rs770715465)" FT /evidence="ECO:0000269|PubMed:24218364" FT /id="VAR_073787" FT VARIANT 2170 FT /note="L -> W (in dbSNP:rs140537885)" FT /evidence="ECO:0000269|PubMed:25393719" FT /id="VAR_076728" FT CONFLICT 476 FT /note="D -> E (in Ref. 2; BAA31653)" FT /evidence="ECO:0000305" FT CONFLICT 562 FT /note="N -> D (in Ref. 5; AAH43583)" FT /evidence="ECO:0000305" FT CONFLICT 1097 FT /note="I -> T (in Ref. 6; BAC86133)" FT /evidence="ECO:0000305" FT CONFLICT 1148 FT /note="T -> I (in Ref. 6; BAC86835)" FT /evidence="ECO:0000305" FT CONFLICT 1227 FT /note="Q -> H (in Ref. 2; BAA31653)" FT /evidence="ECO:0000305" FT CONFLICT 1230 FT /note="T -> A (in Ref. 6; BAC86835)" FT /evidence="ECO:0000305" FT CONFLICT 1269 FT /note="D -> N (in Ref. 6; BAC86133)" FT /evidence="ECO:0000305" FT CONFLICT 2041 FT /note="L -> P (in Ref. 6; BAC86835)" FT /evidence="ECO:0000305" FT CONFLICT 2091 FT /note="T -> A (in Ref. 6; BAC86835)" FT /evidence="ECO:0000305" SQ SEQUENCE 2243 AA; 254415 MW; C6D292837DE1F170 CRC64; MNIIRENKDL ACFYTTKHSW RGKYKRVFSV GTHAITTYNP NTLEVTNQWP YGDICSISPV GKGQGTEFNL TFRKGSGKKS ETLKFSTEHR TELLTEALRF RTDFSEGKIT GRRYNCYKHH WSDSRKPVIL EVTPGGFDQI NPATNRVLCS YDYRNIEGFV DLSDYQGGFC ILYGGFSRLH LFASEQREEI IKSAIDHAGN YIGISLRIRK EPLEFEQYLN LRFGKYSTDE SITSLAEFVV QKISPRHSEP VKRVLALTET CLVERDPATY NIATLKPLGE VFALVCDSEN PQLFTIEFIK GQVRKYSSTE RDSLLASLLD GVRASGNRDV CVKMTPTHKG QRWGLLSMPV DEEVESLHLR FLATPPNGNF ADAVFRFNAN ISYSGVLHAV TQDGLFSENK EKLINNAITA LLSQEGDVVA SNAELESQFQ AVRRLVASKA GFLAFTQLPK FRERLGVKVV KALKRSNNGI IHAAVDMLCA LMCPMHDDYD LRQEQLNKAS LLSSKKFLEN LLEKFNSHVD HGTGALVISS LLDFLTFALC APYSETTEGQ QFDMLLEMVA SNGRTLFKLF QHPSMAIIKG AGLVMKAIIE EGDKEIATKM QELALSEGAL PRHLHTAMFT ISSDQRMLTN RQLSRHLVGL WTADNATATN LLKRILPPGL LAYLESSDLV PEKDADRMHV RDNVKIAMDQ YGKFNKVPEW QRLAGKAAKE VEKFAKEKVD LVLMHWRDRM GIAQKENINQ KPVVLRKRRQ RIKIEANWDL FYYRFGQDHA RSNLIWNFKT REELKDTLES EMRAFNIDRE LGSANVISWN HHEFEVKYEC LAEEIKIGDY YLRLLLEEDE NEESGSIKRS YEFFNELYHR FLLTPKVNMK CLCLQALAIV YGRCHEEIGP FTDTRYIIGM LERCTDKLER DRLILFLNKL ILNKKNVKDL MDSNGIRILV DLLTLAHLHV SRATVPLQSN VIEAAPDMKR ESEKEWYFGN ADKERSGPYG FHEMQELWTK GMLNAKTRCW AQGMDGWRPL QSIPQLKWCL LASGQAVLNE TDLATLILNM LITMCGYFPS RDQDNAIIRP LPKVKRLLSD STCLPHIIQL LLTFDPILVE KVAILLYHIM QDNPQLPRLY LSGVFFFIMM YTGSNVLPVA RFLKYTHTKQ AFKSEETKGQ DIFQRSILGH ILPEAMVCYL ENYEPEKFSE IFLGEFDTPE AIWSSEMRRL MIEKIAAHLA DFTPRLQSNT RALYQYCPIP IINYPQLENE LFCNIYYLKQ LCDTLRFPDW PIKDPVKLLK DTLDAWKKEV EKKPPMMSID DAYEVLNLPQ GQGPHDESKI RKAYFRLAQK YHPDKNPEGR DMFEKVNKAY EFLCTKSAKI VDGPDPENII LILKTQSILF NRHKEDLQPY KYAGYPMLIR TITMETSDDL LFSKESPLLP AATELAFHTV NCSALNAEEL RRENGLEVLQ EAFSRCVAVL TRASKPSDMS VQVCGYISKC YSVAAQFEEC REKITEMPSI IKDLCRVLYF GKSIPRVAAL GVECVSSFAV DFWLQTHLFQ AGILWYLLGF LFNYDYTLEE SGIQKSEETN QQEVANSLAK LSVHALSRLG GYLAEEQATP ENPTIRKSLA GMLTPYVARK LAVASVTEIL KMLNSNTESP YLIWNNSTRA ELLEFLESQQ ENMIKKGDCD KTYGSEFVYS DHAKELIVGE IFVRVYNEVP TFQLEVPKAF AASLLDYIGS QAQYLHTFMA ITHAAKVESE QHGDRLPRVE MALEALRNVI KYNPGSESEC IGHFKLIFSL LRVHGAGQVQ QLALEVVNIV TSNQDCVNNI AESMVLSSLL ALLHSLPSSR QLVLETLYAL TSSTKIIKEA MAKGALIYLL DMFCNSTHPQ VRAQTAELFA KMTADKLIGP KVRITLMKFL PSVFMDAMRD NPEAAVHIFE GTHENPELIW NDNSRDKVST TVREMMLEHF KNQQDNPEAN WKLPEDFAVV FGEAEGELAV GGVFLRIFIA QPAWVLRKPR EFLIALLEKL TELLEKNNPH GETLETLTMA TVCLFSAQPQ LADQVPPLGH LPKVIQAMNH RNNAIPKSAI RVIHALSENE LCVRAMASLE TIGPLMNGMK KRADTVGLAC EAINRMFQKE QSELVAQALK ADLVPYLLKL LEGIGLENLD SPAATKAQIV KALKAMTRSL QYGEQVNEIL CRSSVWSAFK DQKHDLFISE SQTAGYLTGP GVAGYLTAGT STSVMSNLPP PVDHEAGDLG YQT //