ID DUSTY_HUMAN Reviewed; 929 AA. AC Q6XUX3; B7ZL64; O75060; Q17R94; Q5RKT0; Q6IN87; Q6P997; Q86Y03; Q9P1S5; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 17-JUN-2020, entry version 147. DE RecName: Full=Dual serine/threonine and tyrosine protein kinase; DE EC=2.7.12.1; DE AltName: Full=Dusty protein kinase; DE Short=Dusty PK; DE AltName: Full=RIP-homologous kinase; DE AltName: Full=Receptor-interacting serine/threonine-protein kinase 5; DE AltName: Full=Sugen kinase 496; DE Short=SgK496; GN Name=DSTYK; Synonyms=KIAA0472, RIP5, RIPK5, SGK496; ORFNames=HDCMD38P; 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] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=17123648; DOI=10.1016/j.bbaexp.2006.10.004; RA Peng J., Dong W., Chen Y., Mo R., Cheng J.-F., Hui C.-C., Mohandas N., RA Huang C.-H.; RT "Dusty protein kinases: primary structure, gene evolution, tissue specific RT expression and unique features of the catalytic domain."; RL Biochim. Biophys. Acta 1759:562-572(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Dendritic cell; RA Zhao Z., Huang X., Li N., Zhu X., Cao X.; RT "A novel gene from human dendritic cell."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain, Eye, Muscle, Placenta, and Skin; 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-929 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9455484; DOI=10.1093/dnares/4.5.345; RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RT "Characterization of cDNA clones in size-fractionated cDNA libraries from RT human brain."; RL DNA Res. 4:345-349(1997). RN [6] RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-681. RX PubMed=15178406; DOI=10.1016/j.bbrc.2004.04.194; RA Zha J., Zhou Q., Xu L.G., Chen D., Li L., Zhai Z., Shu H.B.; RT "RIP5 is a RIP-homologous inducer of cell death."; RL Biochem. Biophys. Res. Commun. 319:298-303(2004). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [9] RP INVOLVEMENT IN CAKUT1, VARIANTS CAKUT1 GLN-29; GLY-200 AND LEU-843, RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=23862974; DOI=10.1056/nejmoa1214479; RA Sanna-Cherchi S., Sampogna R.V., Papeta N., Burgess K.E., Nees S.N., RA Perry B.J., Choi M., Bodria M., Liu Y., Weng P.L., Lozanovski V.J., RA Verbitsky M., Lugani F., Sterken R., Paragas N., Caridi G., Carrea A., RA Dagnino M., Materna-Kiryluk A., Santamaria G., Murtas C., RA Ristoska-Bojkovska N., Izzi C., Kacak N., Bianco B., Giberti S., RA Gigante M., Piaggio G., Gesualdo L., Kosuljandic Vukic D., Vukojevic K., RA Saraga-Babic M., Saraga M., Gucev Z., Allegri L., Latos-Bielenska A., RA Casu D., State M., Scolari F., Ravazzolo R., Kiryluk K., Al-Awqati Q., RA D'Agati V.D., Drummond I.A., Tasic V., Lifton R.P., Ghiggeri G.M., RA Gharavi A.G.; RT "Mutations in DSTYK and dominant urinary tract malformations."; RL N. Engl. J. Med. 369:621-629(2013). RN [10] RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN SPG23. RX PubMed=28157540; DOI=10.1016/j.ajhg.2017.01.014; RA Lee J.Y., Hsu C.K., Michael M., Nanda A., Liu L., McMillan J.R., RA Pourreyron C., Takeichi T., Tolar J., Reid E., Hayday T., Blumen S.C., RA Abu-Mouch S., Straussberg R., Basel-Vanagaite L., Barhum Y., Zouabi Y., RA Al-Ajmi H., Huang H.Y., Lin T.C., Akiyama M., Lee J.Y., McLean W.H., RA Simpson M.A., Parsons M., McGrath J.A.; RT "Large intragenic deletion in DSTYK underlies autosomal-recessive RT complicated spastic paraparesis, SPG23."; RL Am. J. Hum. Genet. 100:364-370(2017). CC -!- FUNCTION: Acts as a positive regulator of ERK phosphorylation CC downstream of fibroblast growth factor-receptor activation CC (PubMed:23862974, PubMed:28157540). Involved in the regulation of both CC caspase-dependent apoptosis and caspase-independent cell death CC (PubMed:15178406). In the skin, it plays a predominant role in CC suppressing caspase-dependent apoptosis in response to UV stress in a CC range of dermal cell types (PubMed:28157540). CC {ECO:0000269|PubMed:15178406, ECO:0000269|PubMed:23862974, CC ECO:0000269|PubMed:28157540}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.12.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17123648, CC ECO:0000269|PubMed:23862974}. Cell membrane CC {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane CC {ECO:0000269|PubMed:23862974}. Basolateral cell membrane CC {ECO:0000269|PubMed:23862974}. Cell junction CC {ECO:0000250|UniProtKB:Q6XUX1}. Note=Detected at apical cell-cell CC junctions. Colocalized with FGF receptors to the cell membrane (By CC similarity). Detected in basolateral and apical membranes of all CC tubular epithelia. {ECO:0000250|UniProtKB:Q6XUX1, CC ECO:0000269|PubMed:23862974}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6XUX3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6XUX3-2; Sequence=VSP_018034; CC Name=3; CC IsoId=Q6XUX3-3; Sequence=VSP_018031; CC Name=4; CC IsoId=Q6XUX3-4; Sequence=VSP_018030, VSP_018032, VSP_018033; CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and CC testis. Expressed in basolateral and apical membranes of all tubular CC epithelia. Expressed in thin ascending limb of the loop of Henle and CC the distal convoluted tubule. Expressed in all layers of transitional CC ureteric epithelium and in the ureteric smooth-muscle cells. Weakly CC expressed in heart, brain, placenta, kidney, pancreas, spleen, thymus, CC prostate, uterus, small intestine, white blood cells, stomach, spinal CC cord and adrenal gland. Is widely distributed in the CNS. Also detected CC in several tumor cell lines. Expressed in the skin (PubMed:28157540). CC {ECO:0000269|PubMed:15178406, ECO:0000269|PubMed:17123648, CC ECO:0000269|PubMed:23862974, ECO:0000269|PubMed:28157540}. CC -!- DISEASE: Congenital anomalies of the kidney and urinary tract 1 CC (CAKUT1) [MIM:610805]: A disorder encompassing a broad spectrum of CC renal and urinary tract malformations that include renal agenesis, CC kidney hypodysplasia, multicystic kidney dysplasia, duplex collecting CC system, posterior urethral valves and ureter abnormalities. Congenital CC anomalies of kidney and urinary tract are the commonest cause of CC chronic kidney disease in children. {ECO:0000269|PubMed:23862974}. CC Note=Disease susceptibility is associated with variations affecting the CC gene represented in this entry. CC -!- DISEASE: Spastic paraplegia 23, autosomal recessive (SPG23) CC [MIM:270750]: A form of spastic paraplegia, a neurodegenerative CC disorder characterized by a slow, gradual, progressive weakness and CC spasticity of the lower limbs. Rate of progression and the severity of CC symptoms are quite variable. Initial symptoms may include difficulty CC with balance, weakness and stiffness in the legs, muscle spasms, and CC dragging the toes when walking. In some forms of the disorder, bladder CC symptoms (such as incontinence) may appear, or the weakness and CC stiffness may spread to other parts of the body. SPG23 is an autosomal CC recessive form characterized by childhood-onset of gait difficulties CC and pigmentary abnormalities, including premature graying of the hair CC and vitiligo-like or hyperpigmented skin lesions. CC {ECO:0000269|PubMed:28157540}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; AY208850; AAP42418.1; -; mRNA. DR EMBL; AY429674; AAS55390.1; -; mRNA. DR EMBL; AF068286; AAF65505.1; -; mRNA. DR EMBL; AC093422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC048204; AAH48204.1; -; mRNA. DR EMBL; BC053627; AAH53627.1; -; mRNA. DR EMBL; BC060870; AAH60870.2; -; mRNA. DR EMBL; BC072406; AAH72406.1; -; mRNA. DR EMBL; BC117411; AAI17412.1; -; mRNA. DR EMBL; BC143603; AAI43604.1; -; mRNA. DR EMBL; AB007941; BAA32317.1; -; mRNA. DR CCDS; CCDS1451.1; -. [Q6XUX3-1] DR CCDS; CCDS1452.1; -. [Q6XUX3-2] DR RefSeq; NP_056190.1; NM_015375.2. [Q6XUX3-1] DR RefSeq; NP_955749.1; NM_199462.2. [Q6XUX3-2] DR SMR; Q6XUX3; -. DR BioGRID; 117313; 48. DR IntAct; Q6XUX3; 23. DR STRING; 9606.ENSP00000356130; -. DR BindingDB; Q6XUX3; -. DR ChEMBL; CHEMBL1908386; -. DR DrugCentral; Q6XUX3; -. DR iPTMnet; Q6XUX3; -. DR PhosphoSitePlus; Q6XUX3; -. DR BioMuta; DSTYK; -. DR DMDM; 296434486; -. DR EPD; Q6XUX3; -. DR jPOST; Q6XUX3; -. DR MassIVE; Q6XUX3; -. DR MaxQB; Q6XUX3; -. DR PaxDb; Q6XUX3; -. DR PeptideAtlas; Q6XUX3; -. DR PRIDE; Q6XUX3; -. DR ProteomicsDB; 67816; -. [Q6XUX3-1] DR ProteomicsDB; 67817; -. [Q6XUX3-2] DR ProteomicsDB; 67818; -. [Q6XUX3-3] DR ProteomicsDB; 67819; -. [Q6XUX3-4] DR Antibodypedia; 34564; 171 antibodies. DR DNASU; 25778; -. DR Ensembl; ENST00000367161; ENSP00000356129; ENSG00000133059. [Q6XUX3-2] DR Ensembl; ENST00000367162; ENSP00000356130; ENSG00000133059. [Q6XUX3-1] DR Ensembl; ENST00000615388; ENSP00000478016; ENSG00000133059. [Q6XUX3-4] DR GeneID; 25778; -. DR KEGG; hsa:25778; -. DR UCSC; uc001hbw.4; human. [Q6XUX3-1] DR CTD; 25778; -. DR DisGeNET; 25778; -. DR EuPathDB; HostDB:ENSG00000133059.16; -. DR GeneCards; DSTYK; -. DR HGNC; HGNC:29043; DSTYK. DR HPA; ENSG00000133059; Low tissue specificity. DR MalaCards; DSTYK; -. DR MIM; 270750; phenotype. DR MIM; 610805; phenotype. DR MIM; 612666; gene. DR neXtProt; NX_Q6XUX3; -. DR OpenTargets; ENSG00000133059; -. DR Orphanet; 101003; Autosomal recessive spastic paraplegia type 23. DR Orphanet; 93100; Renal agenesis, unilateral. DR PharmGKB; PA164718861; -. DR eggNOG; KOG0192; Eukaryota. DR eggNOG; COG0515; LUCA. DR GeneTree; ENSGT00840000129948; -. DR HOGENOM; CLU_014116_0_0_1; -. DR InParanoid; Q6XUX3; -. DR KO; K16288; -. DR OMA; CIFILGQ; -. DR OrthoDB; 254886at2759; -. DR PhylomeDB; Q6XUX3; -. DR TreeFam; TF331821; -. DR SignaLink; Q6XUX3; -. DR BioGRID-ORCS; 25778; 4 hits in 816 CRISPR screens. DR ChiTaRS; DSTYK; human. DR GeneWiki; RIPK5; -. DR GenomeRNAi; 25778; -. DR Pharos; Q6XUX3; Tchem. DR PRO; PR:Q6XUX3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q6XUX3; protein. DR Bgee; ENSG00000133059; Expressed in parietal lobe and 238 other tissues. DR Genevisible; Q6XUX3; HS. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB. DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0033674; P:positive regulation of kinase activity; IMP:UniProtKB. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF07714; Pkinase_Tyr; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell junction; Cell membrane; KW Coiled coil; Cytoplasm; Disease mutation; Hereditary spastic paraplegia; KW Kinase; Membrane; Neurodegeneration; Nucleotide-binding; Polymorphism; KW Reference proteome; Serine/threonine-protein kinase; Transferase; KW Tyrosine-protein kinase. FT CHAIN 1..929 FT /note="Dual serine/threonine and tyrosine protein kinase" FT /id="PRO_0000233118" FT DOMAIN 652..906 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT NP_BIND 658..666 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT COILED 189..215 FT /evidence="ECO:0000255" FT COILED 395..431 FT /evidence="ECO:0000255" FT COMPBIAS 15..22 FT /note="Poly-Gly" FT COMPBIAS 69..72 FT /note="Poly-Gly" FT ACT_SITE 777 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 681 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT VAR_SEQ 1..539 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_018030" FT VAR_SEQ 451..792 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018031" FT VAR_SEQ 703..718 FT /note="SLPKHERLVDLHGSVI -> WVLASFISMRKIQRRI (in isoform 4)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_018032" FT VAR_SEQ 719..929 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_018033" FT VAR_SEQ 824..868 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018034" FT VARIANT 29 FT /note="R -> Q (in CAKUT1; unknown pathological FT significance; dbSNP:rs200780796)" FT /evidence="ECO:0000269|PubMed:23862974" FT /id="VAR_071324" FT VARIANT 200 FT /note="D -> G (in CAKUT1)" FT /evidence="ECO:0000269|PubMed:23862974" FT /id="VAR_071325" FT VARIANT 432 FT /note="L -> V (in dbSNP:rs35845538)" FT /id="VAR_057101" FT VARIANT 843 FT /note="S -> L (in CAKUT1; dbSNP:rs778586547)" FT /evidence="ECO:0000269|PubMed:23862974" FT /id="VAR_071326" FT MUTAGEN 681 FT /note="K->Q: No change." FT /evidence="ECO:0000269|PubMed:15178406" FT CONFLICT 247 FT /note="V -> A (in Ref. 4; AAH72406)" FT /evidence="ECO:0000305" FT CONFLICT 449 FT /note="G -> R (in Ref. 4; AAH60870)" FT /evidence="ECO:0000305" FT CONFLICT 641 FT /note="C -> R (in Ref. 1; AAP42418/AAS55390, 2; AAF65505, FT 4; AAH53627/AAH72406/AAI17412/AAI43604 and 5; BAA32317)" FT /evidence="ECO:0000305" SQ SEQUENCE 929 AA; 105206 MW; 8DDAAC289DE21EE7 CRC64; MEGDGVPWGS EPVSGPGPGG GGMIRELCRG FGRYRRYLGR LRQNLRETQK FFRDIKCSHN HTCLSSLTGG GGAERGPAGD VAETGLQAGQ LSCISFPPKE EKYLQQIVDC LPCILILGQD CNVKCQLLNL LLGVQVLPTT KLGSEESCKL RRLRFTYGTQ TRVSLALPGQ YELVHTLVAH QGNWETIPEE DLEVQENNED AAHVLAELEV TMHHALLQEV DVVVAPCQGL RPTVDVLGDL VNDFLPVITY ALHKDELSER DEQELQEIRK YFSFPVFFFK VPKLGSEIID SSTRRMESER SPLYRQLIDL GYLSSSHWNC GAPGQDTKAQ SMLVEQSEKL RHLSTFSHQV LQTRLVDAAK ALNLVHCHCL DIFINQAFDM QRDLQITPKR LEYTRKKENE LYESLMNIAN RKQEEMKDMI VETLNTMKEE LLDDATNMEF KDVIVPENGE PVGTREIKCC IRQIQELIIS RLNQAVANKL ISSVDYLRES FVGTLERCLQ SLEKSQDVSV HITSNYLKQI LNAAYHVEVT FHSGSSVTRM LWEQIKQIIQ RITWVSPPAI TLEWKRKVAQ EAIESLSASK LAKSICSQFR TRLNSSHEAF AASLRQLEAG HSGRLEKTED LWLRVRKDHA PRLARLSLES CSLQDVLLHR KPKLGQELGR GQYGVVYLCD NWGGHFPCAL KSVVPPDEKH WNDLALEFHY MRSLPKHERL VDLHGSVIDY NYGGGSSIAV LLIMERLHRD LYTGLKAGLT LETRLQIALD VVEGIRFLHS QGLVHRDIKL KNVLLDKQNR AKITDLGFCK PEAMMSGSIV GTPIHMAPEL FTGKYDNSVD VYAFGILFWY ICSGSVKLPE AFERCASKDH LWNNVRRGAR PERLPVFDEE CWQLMEACWD GDPLKRPLLG IVQPMLQGIM NRLCKSNSEQ PNRGLDDST //