AT132_MOUSE
ID AT132_MOUSE Reviewed; 1169 AA.
AC Q9CTG6; A2AA78; Q8CG98;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Polyamine-transporting ATPase 13A2 {ECO:0000250|UniProtKB:Q9NQ11};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q9NQ11};
GN Name=Atp13a2 {ECO:0000312|MGI:MGI:1922022};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 582-1169.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION.
RX PubMed=27278822; DOI=10.1038/ncomms11803;
RA Bento C.F., Ashkenazi A., Jimenez-Sanchez M., Rubinsztein D.C.;
RT "The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
RT autophagy via a common pathway.";
RL Nat. Commun. 7:11803-11803(2016).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30538141; DOI=10.1083/jcb.201804165;
RA Wang R., Tan J., Chen T., Han H., Tian R., Tan Y., Wu Y., Cui J., Chen F.,
RA Li J., Lv L., Guan X., Shang S., Lu J., Zhang Z.;
RT "ATP13A2 facilitates HDAC6 recruitment to lysosome to promote
RT autophagosome-lysosome fusion.";
RL J. Cell Biol. 218:267-284(2019).
CC -!- FUNCTION: ATPase which acts as a lysosomal polyamine exporter with high
CC affinity for spermine (By similarity). Also stimulates cellular uptake
CC of polyamines and protects against polyamine toxicity (By similarity).
CC Plays a role in intracellular cation homeostasis and the maintenance of
CC neuronal integrity (By similarity). Contributes to cellular zinc
CC homeostasis (By similarity). Confers cellular protection against Mn(2+)
CC and Zn(2+) toxicity and mitochondrial stress (By similarity). Required
CC for proper lysosomal and mitochondrial maintenance (By similarity).
CC Regulates the autophagy-lysosome pathway through the control of SYT11
CC expression at both transcriptional and post-translational levels
CC (PubMed:27278822). Facilitates recruitment of deacetylase HDAC6 to
CC lysosomes to deacetylate CTTN, leading to actin polymerization,
CC promotion of autophagosome-lysosome fusion and completion of autophagy
CC (PubMed:30538141). Promotes secretion of exosomes as well as secretion
CC of SCNA via exosomes (By similarity). Plays a role in lipid homeostasis
CC (By similarity). {ECO:0000250|UniProtKB:Q9NQ11,
CC ECO:0000269|PubMed:27278822, ECO:0000269|PubMed:30538141}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + spermidine(out) = ADP + H(+) + phosphate +
CC spermidine(in); Xref=Rhea:RHEA:29999, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9NQ11};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + spermine(out) = ADP + H(+) + phosphate +
CC spermine(in); Xref=Rhea:RHEA:63368, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:45725, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9NQ11};
CC -!- ACTIVITY REGULATION: Accumulates in an inactive autophosphorylated
CC state. The presence of spermine results in a dose-dependent reduction
CC in autophosphorylation. {ECO:0000250|UniProtKB:Q9NQ11}.
CC -!- SUBUNIT: Interacts with MYCBP2; the interaction inhibits the
CC ubiquitination of TSC2 by MYCBP2 (By similarity). Interacts with HDAC6;
CC the interaction results in recruitment of HDAC6 to lysosomes to promote
CC CTTN deacetylation (By similarity). {ECO:0000250|UniProtKB:Q9NQ11}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9NQ11};
CC Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The N-terminal region is required for targeting to late
CC endosomes/lysosomes. It does not traverse the membrane but contains a
CC membrane-embedded intramembrane domain and interacts with the lipids
CC phosphatidic acid (PA) and phosphatidylinositol 3,5-bisphosphate
CC (PI(3,5)P2). PA and PI(3,5)P2 are required for the protective effect
CC against mitochondrial stress. {ECO:0000250|UniProtKB:Q9NQ11}.
CC -!- PTM: Autophosphorylated. Accumulates in an inactive autophosphorylated
CC state and autophosphorylation is stimulated by phosphatidic acid and
CC phosphatidylinositol 3,5-bisphosphate but not by Mn(2+) or Zn(2+). The
CC presence of spermine results in a dose-dependent reduction in
CC autophosphorylation. {ECO:0000250|UniProtKB:Q9NQ11}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype at 4 months
CC (PubMed:30538141). At 10 months, gradual loss of body weight, increased
CC liver size and reduced adipose tissue mass (PubMed:30538141). These
CC phenotypes further progress to 18 months with significantly smaller
CC body size, hepatomegaly, increased intracellular vacuolation in liver
CC tissues, markedly reduced adipose tissue with small adipocytes,
CC accumulation of autophagy receptor Sqstm1/p62 and autophagy-related
CC protein LC3 in liver, and accumulation of ubiquitinated insoluble
CC proteins (PubMed:30538141). {ECO:0000269|PubMed:30538141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
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DR EMBL; AL645625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042661; AAH42661.1; -; mRNA.
DR EMBL; AK003623; BAB22896.1; -; mRNA.
DR CCDS; CCDS18859.1; -.
DR RefSeq; NP_083373.2; NM_029097.2.
DR AlphaFoldDB; Q9CTG6; -.
DR SMR; Q9CTG6; -.
DR STRING; 10090.ENSMUSP00000039648; -.
DR GlyGen; Q9CTG6; 1 site.
DR iPTMnet; Q9CTG6; -.
DR PhosphoSitePlus; Q9CTG6; -.
DR SwissPalm; Q9CTG6; -.
DR MaxQB; Q9CTG6; -.
DR PaxDb; Q9CTG6; -.
DR PRIDE; Q9CTG6; -.
DR ProteomicsDB; 277083; -.
DR Antibodypedia; 29290; 198 antibodies from 24 providers.
DR DNASU; 74772; -.
DR Ensembl; ENSMUST00000037055; ENSMUSP00000039648; ENSMUSG00000036622.
DR GeneID; 74772; -.
DR KEGG; mmu:74772; -.
DR UCSC; uc008vnn.2; mouse.
DR CTD; 23400; -.
DR MGI; MGI:1922022; Atp13a2.
DR VEuPathDB; HostDB:ENSMUSG00000036622; -.
DR eggNOG; KOG0208; Eukaryota.
DR GeneTree; ENSGT00940000159714; -.
DR InParanoid; Q9CTG6; -.
DR OMA; SGWKDPL; -.
DR OrthoDB; 172453at2759; -.
DR PhylomeDB; Q9CTG6; -.
DR TreeFam; TF300331; -.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 74772; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Atp13a2; mouse.
DR PRO; PR:Q9CTG6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9CTG6; protein.
DR Bgee; ENSMUSG00000036622; Expressed in embryonic brain and 252 other tissues.
DR ExpressionAtlas; Q9CTG6; baseline and differential.
DR Genevisible; Q9CTG6; MM.
DR GO; GO:0005776; C:autophagosome; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1905103; C:integral component of lysosomal membrane; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0012506; C:vesicle membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0015417; F:ABC-type polyamine transporter activity; 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:0070300; F:phosphatidic acid binding; ISO:MGI.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:MGI.
DR GO; GO:1905037; P:autophagosome organization; ISO:MGI.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISO:MGI.
DR GO; GO:0071287; P:cellular response to manganese ion; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; ISO:MGI.
DR GO; GO:0097734; P:extracellular exosome biogenesis; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
DR GO; GO:1990938; P:peptidyl-aspartic acid autophosphorylation; ISO:MGI.
DR GO; GO:1902047; P:polyamine transmembrane transport; ISO:MGI.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0061462; P:protein localization to lysosome; IMP:UniProtKB.
DR GO; GO:0016243; P:regulation of autophagosome size; ISO:MGI.
DR GO; GO:0052548; P:regulation of endopeptidase activity; ISO:MGI.
DR GO; GO:1905123; P:regulation of glucosylceramidase activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0033157; P:regulation of intracellular protein transport; NAS:ParkinsonsUK-UCL.
DR GO; GO:1905165; P:regulation of lysosomal protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:MGI.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:2000152; P:regulation of ubiquitin-specific protease activity; ISS:UniProtKB.
DR GO; GO:1903710; P:spermine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0055069; P:zinc ion homeostasis; IMP:ParkinsonsUK-UCL.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
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; PF12409; P5-ATPase; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 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; 2.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasmic vesicle; Endosome; Glycoprotein; Lysosome;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1169
FT /note="Polyamine-transporting ATPase 13A2"
FT /id="PRO_0000046424"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT INTRAMEM 45..65
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..250
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..458
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 920..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..946
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 947..967
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 968..993
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 994..1014
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1015..1037
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1059..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1091..1106
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT TRANSMEM 1107..1127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1128..1169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT ACT_SITE 508
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT BINDING 867
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 871
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 1022
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 112
FT /note="V -> L (in Ref. 2; AAH42661)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="G -> S (in Ref. 2; AAH42661)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="I -> V (in Ref. 2; AAH42661)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="T -> A (in Ref. 2; AAH42661)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="C -> R (in Ref. 2; AAH42661)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="A -> E (in Ref. 2; AAH42661)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="S -> F (in Ref. 2; AAH42661)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="I -> V (in Ref. 3; BAB22896)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1169 AA; 126443 MW; 35458FE5B45FEFBE CRC64;
MSADSSLLMG STPPSYGTLT TGTSIDPLSS SASSVRLSGY CGSPWRAIGY HAAVWMLAGI
PWLLFRWKPL WGVRLRLKPC SLAHAETLVI EIKDKEGSSR QLFTVQVQTE AVVQGSLELP
PQAQAEDGRS QAAVGVTPEG TWQDTSELHR QEEAKQVLRY YVLQGQRYVW METQQAFCQV
SLLDHGRTCD DVHCSSSGLS LQDQATRKTI YGPNVISIPV KSYLQLLADE ALNPYYGFQA
FSIALWLADH YYWYALCIFL ISAISICLAL YKTRKQSLTL RDMVKLSVRV QVCRPGGEEE
WVDSSELVPG DCLVLPQEGG VMPCDAALVA GECVVNESSL TGESTPVLKT ALPEGPKPYC
PETHRRHTLF CGTLILQARA YVGPRVLAVV TRTGFCTAKG GLVSSILHPR PISFKFYKHS
MKFVAALSVL ALLGTVYSII ILYRNRVPVR EIVIRALDLV TVVVPPALPA AMTVCTLYAQ
SRLRTQGIFC IHPLRINLGG KLRLVCFDKT GTLTEDGLDV MGVVPLKGQV LLPLVPEPCH
LPLGPLLRAL ATCHALSQLH DTPVGDPMDL KMVESTGWVL EEGPAAGSAP GSQVLVVMRP
PPGGPRQQEE PPVPVSVLCR FPFSSALQRM DVVVTWPGAT QPEAYVKGSP ELVASLCSPE
TVPSDFSQVL QSYTAAGYRV VALAGKPLPI APSLAAAQQL TRDTVERELS LLGLLVMRNL
LKPQTAPVIQ TLRKTGIRTV MVTGDNLQTA VTVARACGMV GAQEHLAVIH ATHPEQGQPA
ALEFLPTESS AVMNGAKATG YPTVPEPQSC HLALSGSTFA VLRKHFPKLL PKVLVQATVF
ARMAPEQKTE LVCELQRLQY CVGMCGDGAN DCGALKAADV GISLSQAEAS VVSPFTSSMA
SIECVPTVIR EGRCSLDTSF SVFKYMALYS LTQFISVLIL YTINTNLGDL QFLAIDLVIT
TTVAVLMSRT GPALTLVRAR PPGALLSVPV LGSLLLQVAL VAGIQLGGYF LVIAQPWFVP
LNRTVPAPDN LPNYENTVVF SLSGFQYLIL AAAVSKGAPF RQPLYTNVPF LVALALLGSV
LVGLILVPGL LQGPLGLRNI VDSSFKLLLL GLVAFNFVGA FMLESVLDQC LPACLRWLRP
KRASKKQFKR LQQELAEHPW PTLPVGSVR
