ID AT134_HUMAN Reviewed; 1196 AA. AC Q4VNC1; B7WPC7; Q6UY23; Q8N1Q9; Q9H043; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 24-JAN-2024, entry version 141. DE RecName: Full=Probable cation-transporting ATPase 13A4; DE EC=7.2.2.-; DE AltName: Full=P5-ATPase isoform 4; GN Name=ATP13A4; ORFNames=UNQ3052/PRO9871; 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), TISSUE SPECIFICITY, INDUCTION, RP CHROMOSOMAL REARRANGEMENT, AND VARIANTS MET-181; ALA-353 AND ASP-646. RX PubMed=15925480; DOI=10.1016/j.ygeno.2005.04.002; RA Kwasnicka-Crawford D.A., Carson A.R., Roberts W., Summers A.M., RA Rehnstrom K., Jarvela I., Scherer S.W.; RT "Characterization of a novel cation transporter ATPase gene (ATP13A4) RT interrupted by 3q25-q29 inversion in an individual with language delay."; RL Genomics 86:182-194(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Tongue; 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 [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] (ISOFORM 2). RC TISSUE=Brain; 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 287-1196 (ISOFORM 3). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP TISSUE SPECIFICITY. RX PubMed=29505581; DOI=10.1371/journal.pone.0193228; RA Soerensen D.M., Holemans T., van Veen S., Martin S., Arslan T., RA Haagendahl I.W., Holen H.W., Hamouda N.N., Eggermont J., Palmgren M., RA Vangheluwe P.; RT "Parkinson disease related ATP13A2 evolved early in animal evolution."; RL PLoS ONE 13:e0193228-e0193228(2018). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC -!- SUBCELLULAR LOCATION: Early endosome membrane CC {ECO:0000250|UniProtKB:Q5XF90}; Multi-pass membrane protein CC {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q5XF90}; CC Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane CC {ECO:0000250|UniProtKB:Q5XF90}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q4VNC1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q4VNC1-2; Sequence=VSP_031261; CC Name=3; CC IsoId=Q4VNC1-3; Sequence=VSP_031259, VSP_031260; CC Name=4; CC IsoId=Q4VNC1-4; Sequence=VSP_031258; CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, liver, skeletal CC muscles, and pancreas. Lower levels of expression are also detected in CC brain, lung and kidney. Weakly expressed in the adult brain. Expression CC in fetal brain is higher than in adult brain, with levels similar to CC several other fetal tissues including spleen and skeletal muscle. In CC adult brain expressed at low levels in all tissues examined, including CC the temporal lobe and putamen (PubMed:15925480). Highly expressed in CC the respiratory and integumentary systems (PubMed:29505581). CC {ECO:0000269|PubMed:15925480, ECO:0000269|PubMed:29505581}. CC -!- INDUCTION: Decreased by half in the SLI patient lymphoblasts. CC {ECO:0000269|PubMed:15925480}. CC -!- DISEASE: Note=A chromosomal aberration involving ATP13A4 is found in 2 CC patients with specific language impairment (SLI) disorders. Paracentric CC inversion inv(3)(q25;q29). The inversion produces a disruption of the CC protein. {ECO:0000269|PubMed:15925480}. CC -!- MISCELLANEOUS: [Isoform 2]: Dubious isoform lacking mature mRNA CC evidence. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type V subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAC21667.2; Type=Erroneous translation; Note=Wrong choice of CDS.; 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; AY823162; AAX24102.1; -; mRNA. DR EMBL; AY358110; AAQ88477.1; -; mRNA. DR EMBL; AK095277; BAC04520.1; -; mRNA. DR EMBL; AC048351; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092942; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC101496; AAI01497.1; -; mRNA. DR EMBL; AL512736; CAC21667.2; ALT_SEQ; mRNA. DR CCDS; CCDS3304.2; -. [Q4VNC1-1] DR RefSeq; NP_115655.2; NM_032279.3. [Q4VNC1-1] DR AlphaFoldDB; Q4VNC1; -. DR SMR; Q4VNC1; -. DR BioGRID; 123970; 1. DR IntAct; Q4VNC1; 1. DR STRING; 9606.ENSP00000339182; -. DR TCDB; 3.A.3.10.20; the p-type atpase (p-atpase) superfamily. DR iPTMnet; Q4VNC1; -. DR PhosphoSitePlus; Q4VNC1; -. DR BioMuta; ATP13A4; -. DR DMDM; 296439435; -. DR jPOST; Q4VNC1; -. DR MassIVE; Q4VNC1; -. DR PaxDb; 9606-ENSP00000339182; -. DR PeptideAtlas; Q4VNC1; -. DR ProteomicsDB; 62311; -. [Q4VNC1-1] DR ProteomicsDB; 62312; -. [Q4VNC1-2] DR ProteomicsDB; 62313; -. [Q4VNC1-3] DR Antibodypedia; 56173; 7 antibodies from 5 providers. DR Ensembl; ENST00000295548.3; ENSP00000295548.3; ENSG00000127249.15. [Q4VNC1-3] DR Ensembl; ENST00000342695.9; ENSP00000339182.4; ENSG00000127249.15. [Q4VNC1-1] DR Ensembl; ENST00000400270.6; ENSP00000383129.2; ENSG00000127249.15. [Q4VNC1-4] DR GeneID; 84239; -. DR KEGG; hsa:84239; -. DR MANE-Select; ENST00000342695.9; ENSP00000339182.4; NM_032279.4; NP_115655.2. DR UCSC; uc003ftd.4; human. [Q4VNC1-1] DR AGR; HGNC:25422; -. DR CTD; 84239; -. DR DisGeNET; 84239; -. DR GeneCards; ATP13A4; -. DR HGNC; HGNC:25422; ATP13A4. DR HPA; ENSG00000127249; Tissue enhanced (epididymis, parathyroid gland, thyroid gland). DR MIM; 609556; gene. DR neXtProt; NX_Q4VNC1; -. DR OpenTargets; ENSG00000127249; -. DR PharmGKB; PA134979581; -. DR VEuPathDB; HostDB:ENSG00000127249; -. DR eggNOG; KOG0208; Eukaryota. DR GeneTree; ENSGT00940000159448; -. DR HOGENOM; CLU_1299363_0_0_1; -. DR InParanoid; Q4VNC1; -. DR OMA; TTWEMAV; -. DR OrthoDB; 6047at2759; -. DR PhylomeDB; Q4VNC1; -. DR TreeFam; TF300331; -. DR PathwayCommons; Q4VNC1; -. DR Reactome; R-HSA-936837; Ion transport by P-type ATPases. DR SignaLink; Q4VNC1; -. DR BioGRID-ORCS; 84239; 16 hits in 1146 CRISPR screens. DR ChiTaRS; ATP13A4; human. DR GenomeRNAi; 84239; -. DR Pharos; Q4VNC1; Tdark. DR PRO; PR:Q4VNC1; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q4VNC1; Protein. DR Bgee; ENSG00000127249; Expressed in pancreatic ductal cell and 157 other cell types or tissues. DR ExpressionAtlas; Q4VNC1; baseline and differential. DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro. DR GO; GO:0015203; F:polyamine transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central. DR GO; GO:0034220; P:monoatomic ion transmembrane transport; TAS:Reactome. DR GO; GO:1902047; P:polyamine transmembrane transport; IBA:GO_Central. DR CDD; cd07542; P-type_ATPase_cation; 1. DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1. DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1. DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2. DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N. DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR006544; P-type_TPase_V. DR InterPro; IPR047819; P5A-ATPase_N. DR InterPro; IPR047821; P5B-type_ATPase. DR InterPro; IPR001757; P_typ_ATPase. DR InterPro; IPR044492; P_typ_ATPase_HD_dom. DR NCBIfam; TIGR01494; ATPase_P-type; 3. DR NCBIfam; TIGR01657; P-ATPase-V; 1. DR PANTHER; PTHR45630:SF1; CATION-TRANSPORTING ATPASE 13A4-RELATED; 1. DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1. DR Pfam; PF13246; Cation_ATPase; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF12409; P5-ATPase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00121; NAKATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. DR SFLD; SFLDF00027; p-type_atpase; 1. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1. DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. DR Genevisible; Q4VNC1; HS. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Chromosomal rearrangement; Endosome; KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome; KW Translocase; Transmembrane; Transmembrane helix. FT CHAIN 1..1196 FT /note="Probable cation-transporting ATPase 13A4" FT /id="PRO_0000318675" FT TOPO_DOM 1..31 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT INTRAMEM 32..52 FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TOPO_DOM 53..197 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 198..218 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 219..223 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 224..244 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 245..400 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 401..421 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 422..436 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 437..457 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 458..900 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 901..921 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 922..932 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 933..953 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 954..972 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 973..993 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 994..1035 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 1036..1056 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1057..1070 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 1071..1091 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1092..1109 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT TRANSMEM 1110..1130 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1131..1196 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q5XF90" FT ACT_SITE 486 FT /note="4-aspartylphosphate intermediate" FT /evidence="ECO:0000250" FT BINDING 848 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 852 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT VAR_SEQ 1..984 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_031258" FT VAR_SEQ 559..576 FT /note="EMAFSGDDFHIKGVPAHA -> VSLCSSENLRSFFNARAT (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_031259" FT VAR_SEQ 577..1196 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_031260" FT VAR_SEQ 841..1196 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_031261" FT VARIANT 181 FT /note="I -> M (in dbSNP:rs6788448)" FT /evidence="ECO:0000269|PubMed:15925480" FT /id="VAR_038849" FT VARIANT 353 FT /note="V -> A" FT /evidence="ECO:0000269|PubMed:15925480" FT /id="VAR_038850" FT VARIANT 646 FT /note="E -> D (in dbSNP:rs35424709)" FT /evidence="ECO:0000269|PubMed:15925480" FT /id="VAR_038851" FT CONFLICT 840 FT /note="D -> E (in Ref. 3; BAC04520 and 5; AAI01497)" FT /evidence="ECO:0000305" FT CONFLICT 975 FT /note="V -> A (in Ref. 1; AAX24102)" FT /evidence="ECO:0000305" SQ SEQUENCE 1196 AA; 133987 MW; 1D7F81F2BC266663 CRC64; MGHFEKGQHA LLNEGEENEM EIFGYRTQGC RKSLCLAGSI FSFGILPLVF YWRPAWHVWA HCVPCSLQEA DTVLLRTTDE FQIYSWKKVI WIYLSALNSA FGLTPDHPLM TDEEYIINRA IRKPDLKVRC IKVQKIRYVW NYLEGQFQKI GSLEDWLSSA KIHQKFGSGL TREEQEIRRL ICGPNTIDVE VTPIWKLLIK EVLNPFYIFQ LFSVCLWFSE DYKEYAFAII IMSIISISLT VYDLREQSVK LHHLVESHNS ITVSVCGRKA GVQELESRVL VPGDLLILTG NKVLMPCDAV LIEGSCVVDE GMLTGESIPV TKTPLPKMDS SVPWKTQSEA DYKRHVLFCG TEVIQAKAAC SGTVRAVVLQ TGFNTAKGDL VRSILYPKPV NFQLYRDAIR FLLCLVGTAT IGMIYTLCVY VLSGEPPEEV VRKALDVITI AVPPALPAAL TTGIIYAQRR LKKRGIFCIS PQRINVCGQL NLVCFDKTGT LTRDGLDLWG VVSCDRNGFQ EVHSFASGQA LPWGPLCAAM ASCHSLILLD GTIQGDPLDL KMFEATTWEM AFSGDDFHIK GVPAHAMVVK PCRTASQVPV EGIAILHQFP FSSALQRMTV IVQEMGGDRL AFMKGAPERV ASFCQPETVP TSFVSELQIY TTQGFRVIAL AYKKLENDHH ATTLTRETVE SDLIFLGLLI LENRLKEETK PVLEELISAR IRTVMITGDN LQTAITVARK SGMVSESQKV ILIEANETTG SSSASISWTL VEEKKHIMYG NQDNYINIRD EVSDKGREGS YHFALTGKSF HVISQHFSSL LPKILINGTI FARMSPGQKS SLVEEFQKLD YFVGMCGDGA NDCGALKMAH VGISLSEQEA SVASPFTSKT PNIECVPHLI KEGRAALVTS FCMFKYMALY SMIQYVGVLL LYWETNSLSN YQFLFQDLAI TTLIGVTMNL NGAYPKLVPF RPAGRLISPP LLLSVIFNIL LSLAMHIAGF ILVQRQPWYS VEIHSACTVQ NESISELTMS PTAPEKMESN STFTSFENTT VWFLGTINCI TVALVFSKGK PFRQPTYTNY IFVLVLIIQL GVCLFILFAD IPELYRRLDL LCTPVLWRAS IVIMLSLNFI VSLVAEEAVI ENRALWMMIK RCFGYQSKSQ YRIWQRDLAN DPSWPPLNQT SHSDMPECGR GVSYSNPVFE SNEEQL //