AT134_HUMAN
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 03-AUG-2022, entry version 134.
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};
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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; Q4VNC1; -.
DR PeptideAtlas; Q4VNC1; -.
DR PRIDE; Q4VNC1; -.
DR ProteomicsDB; 62311; -. [Q4VNC1-1]
DR ProteomicsDB; 62312; -. [Q4VNC1-2]
DR ProteomicsDB; 62313; -. [Q4VNC1-3]
DR Antibodypedia; 56173; 3 antibodies from 2 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 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; QELESHH; -.
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; 12 hits in 1062 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 155 other tissues.
DR ExpressionAtlas; Q4VNC1; baseline and differential.
DR Genevisible; Q4VNC1; HS.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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 cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
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
