AMPQ_HUMAN
ID AMPQ_HUMAN Reviewed; 990 AA.
AC Q6Q4G3; A8K6J0; C9JGD2; Q32MR1; Q4G0I9; Q4G0V2; Q86XA3; Q8NBZ2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Aminopeptidase Q {ECO:0000305};
DE Short=AP-Q {ECO:0000305};
DE Short=APQ {ECO:0000303|PubMed:17525158};
DE EC=3.4.11.- {ECO:0000269|PubMed:17525158};
DE AltName: Full=CHL2 antigen {ECO:0000303|PubMed:14706636};
DE AltName: Full=Laeverin {ECO:0000303|PubMed:14706636};
GN Name=LVRN {ECO:0000312|HGNC:HGNC:26904};
GN Synonyms=AQPEP {ECO:0000312|HGNC:HGNC:26904};
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), PROTEIN SEQUENCE OF 2-12; 269-277;
RP 590-599; 811-820 AND 838-847, POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14706636; DOI=10.1016/j.bbrc.2003.12.024;
RA Fujiwara H., Higuchi T., Yamada S., Hirano T., Sato Y., Nishioka Y.,
RA Yoshioka S., Tatsumi K., Ueda M., Maeda M., Fujii S.;
RT "Human extravillous trophoblasts express laeverin, a novel protein that
RT belongs to membrane-bound gluzincin metallopeptidases.";
RL Biochem. Biophys. Res. Commun. 313:962-968(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 435-990, AND VARIANT PHE-689.
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-689.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP VARIANT PHE-689.
RC TISSUE=Placenta, and Testis;
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 PROTEIN SEQUENCE OF 65-74, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND TOPOLOGY.
RX PubMed=17525158; DOI=10.1074/jbc.m702650200;
RA Maruyama M., Hattori A., Goto Y., Ueda M., Maeda M., Fujiwara H.,
RA Tsujimoto M.;
RT "Laeverin/aminopeptidase Q, a novel bestatin-sensitive leucine
RT aminopeptidase belonging to the M1 family of aminopeptidases.";
RL J. Biol. Chem. 282:20088-20096(2007).
CC -!- FUNCTION: Metalloprotease which may be important for placentation by
CC regulating biological activity of key peptides at the embryo-maternal
CC interface. On synthetic substrates it shows a marked preference for
CC Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-
CC LCA. Cleaves the N-terminal amino acid of several peptides such as
CC angiotensin-3, kisspeptin-10 and endokinin C.
CC {ECO:0000269|PubMed:17525158}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by bestatin.
CC {ECO:0000269|PubMed:17525158}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=78.2 uM for Leu-4-methylcoumaryl-7-amide
CC {ECO:0000269|PubMed:17525158};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:17525158};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17525158}.
CC -!- INTERACTION:
CC Q6Q4G3-4; P28799: GRN; NbExp=3; IntAct=EBI-25862057, EBI-747754;
CC Q6Q4G3-4; O76024: WFS1; NbExp=3; IntAct=EBI-25862057, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000303|PubMed:17525158}; Single-
CC pass type II membrane protein {ECO:0000303|PubMed:17525158}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6Q4G3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6Q4G3-2; Sequence=VSP_019919, VSP_019920;
CC Name=3;
CC IsoId=Q6Q4G3-3; Sequence=VSP_019915, VSP_019918, VSP_019921;
CC Name=4;
CC IsoId=Q6Q4G3-4; Sequence=VSP_019915, VSP_019916, VSP_019917;
CC -!- TISSUE SPECIFICITY: Specifically expressed in placenta and not in other
CC tissues. Mainly found at the cell surface region of the extravillous
CC trophoblasts. Detected on extravillous trophoblasts in the outer layer
CC of the chorion laeve in the fetal membrane Not detected on either fetal
CC amnionic epithelial cells or maternal decidual cells. Also detected in
CC the migrating extravillous trophoblasts in the maternal decidual
CC tissues (at protein level). {ECO:0000269|PubMed:14706636}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17525158}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11422.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY560010; AAS66719.1; -; mRNA.
DR EMBL; AK075131; BAC11422.1; ALT_INIT; mRNA.
DR EMBL; AK291655; BAF84344.1; -; mRNA.
DR EMBL; AC010282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW48946.1; -; Genomic_DNA.
DR EMBL; BC036440; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC045809; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC068560; AAH68560.1; -; mRNA.
DR EMBL; BC070028; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC094716; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC109022; AAI09023.1; -; mRNA.
DR EMBL; BC109023; AAI09024.1; -; mRNA.
DR CCDS; CCDS4124.1; -. [Q6Q4G3-1]
DR RefSeq; NP_776161.3; NM_173800.4. [Q6Q4G3-1]
DR AlphaFoldDB; Q6Q4G3; -.
DR SMR; Q6Q4G3; -.
DR BioGRID; 128502; 3.
DR IntAct; Q6Q4G3; 3.
DR STRING; 9606.ENSP00000350541; -.
DR ChEMBL; CHEMBL3831223; -.
DR MEROPS; M01.026; -.
DR GlyGen; Q6Q4G3; 8 sites.
DR iPTMnet; Q6Q4G3; -.
DR PhosphoSitePlus; Q6Q4G3; -.
DR BioMuta; LVRN; -.
DR DMDM; 296439457; -.
DR MassIVE; Q6Q4G3; -.
DR PaxDb; Q6Q4G3; -.
DR PeptideAtlas; Q6Q4G3; -.
DR PRIDE; Q6Q4G3; -.
DR ProteomicsDB; 67267; -. [Q6Q4G3-1]
DR ProteomicsDB; 67268; -. [Q6Q4G3-2]
DR ProteomicsDB; 67269; -. [Q6Q4G3-3]
DR ProteomicsDB; 67270; -. [Q6Q4G3-4]
DR Antibodypedia; 25460; 24 antibodies from 10 providers.
DR DNASU; 206338; -.
DR Ensembl; ENST00000357872.9; ENSP00000350541.4; ENSG00000172901.21. [Q6Q4G3-1]
DR Ensembl; ENST00000503329.5; ENSP00000427418.1; ENSG00000172901.21. [Q6Q4G3-4]
DR Ensembl; ENST00000504467.5; ENSP00000423604.1; ENSG00000172901.21. [Q6Q4G3-2]
DR Ensembl; ENST00000512314.5; ENSP00000427500.1; ENSG00000172901.21. [Q6Q4G3-4]
DR Ensembl; ENST00000514509.5; ENSP00000427574.1; ENSG00000172901.21. [Q6Q4G3-3]
DR GeneID; 206338; -.
DR KEGG; hsa:206338; -.
DR MANE-Select; ENST00000357872.9; ENSP00000350541.4; NM_173800.5; NP_776161.3.
DR UCSC; uc003kro.4; human. [Q6Q4G3-1]
DR CTD; 206338; -.
DR DisGeNET; 206338; -.
DR GeneCards; LVRN; -.
DR HGNC; HGNC:26904; LVRN.
DR HPA; ENSG00000172901; Group enriched (adipose tissue, placenta).
DR MIM; 610046; gene.
DR neXtProt; NX_Q6Q4G3; -.
DR OpenTargets; ENSG00000172901; -.
DR VEuPathDB; HostDB:ENSG00000172901; -.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000160535; -.
DR InParanoid; Q6Q4G3; -.
DR OMA; VSMKVEN; -.
DR PhylomeDB; Q6Q4G3; -.
DR PathwayCommons; Q6Q4G3; -.
DR SABIO-RK; Q6Q4G3; -.
DR SignaLink; Q6Q4G3; -.
DR BioGRID-ORCS; 206338; 4 hits in 1032 CRISPR screens.
DR ChiTaRS; LVRN; human.
DR GenomeRNAi; 206338; -.
DR Pharos; Q6Q4G3; Tbio.
DR PRO; PR:Q6Q4G3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q6Q4G3; protein.
DR Bgee; ENSG00000172901; Expressed in decidua and 114 other tissues.
DR ExpressionAtlas; Q6Q4G3; baseline and differential.
DR Genevisible; Q6Q4G3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:14706636"
FT CHAIN 2..990
FT /note="Aminopeptidase Q"
FT /id="PRO_0000247068"
FT TOPO_DOM 2..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000303|PubMed:17525158"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..990
FT /note="Lumenal"
FT /evidence="ECO:0000303|PubMed:17525158"
FT REGION 48..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 503
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 379..383
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 503
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..483
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019915"
FT VAR_SEQ 680..681
FT /note="AI -> MR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019916"
FT VAR_SEQ 682..990
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019917"
FT VAR_SEQ 698..709
FT /note="KNNYIEIETALE -> NLQDFGHLKVPN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019918"
FT VAR_SEQ 698..701
FT /note="KNNY -> KGTY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019919"
FT VAR_SEQ 702..990
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019920"
FT VAR_SEQ 710..990
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019921"
FT VARIANT 640
FT /note="V -> F (in dbSNP:rs17138632)"
FT /id="VAR_027059"
FT VARIANT 689
FT /note="L -> F (in dbSNP:rs10078759)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_027060"
FT VARIANT 936
FT /note="V -> I (in dbSNP:rs17138681)"
FT /id="VAR_027061"
FT CONFLICT 13
FT /note="R -> H (in Ref. 1; AAS66719)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="L -> S (in Ref. 1; AAS66719, 2; BAF84344, 4;
FT EAW48946 and 5; AAH68560/AAI09023/AAI09024)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="P -> S (in Ref. 1; AAS66719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 990 AA; 113283 MW; 570A7072E66D0DCA CRC64;
MGPPSSSGFY VSRAVALLLA GLVAALLLAL AVLAALYGHC ERVPPSELPG LRDLEAESSP
PLRQKPTPTP KPSSARELAV TTTPSNWRPP GPWDQLRLPP WLVPLHYDLE LWPQLRPDEL
PAGSLPFTGR VNITVRCTVA TSRLLLHSLF QDCERAEVRG PLSPGTGNAT VGRVPVDDVW
FALDTEYMVL ELSEPLKPGS SYELQLSFSG LVKEDLREGL FLNVYTDQGE RRALLASQLE
PTFARYVFPC FDEPALKATF NITMIHHPSY VALSNMPKLG QSEKEDVNGS KWTVTTFSTT
PHMPTYLVAF VICDYDHVNR TERGKEIRIW ARKDAIANGS ADFALNITGP IFSFLEDLFN
ISYSLPKTDI IALPSFDNHA MENWGLMIFD ESGLLLEPKD QLTEKKTLIS YVVSHEIGHQ
WFGNLVTMNW WNNIWLNEGF ASYFEFEVIN YFNPKLPRNE IFFSNILHNI LREDHALVTR
AVAMKVENFK TSEIQELFDI FTYSKGASMA RMLSCFLNEH LFVSALKSYL KTFSYSNAEQ
DDLWRHFQMA IDDQSTVILP ATIKNIMDSW THQSGFPVIT LNVSTGVMKQ EPFYLENIKN
RTLLTSNDTW IVPILWIKNG TTQPLVWLDQ SSKVFPEMQV SDSDHDWVIL NLNMTGYYRV
NYDKLGWKKL NQQLEKDPKA IPVIHRLQLI DDAFSLSKNN YIEIETALEL TKYLAEEDEI
IVWHTVLVNL VTRDLVSEVN IYDIYSLLKR YLLKRLNLIW NIYSTIIREN VLALQDDYLA
LISLEKLFVT ACWLGLEDCL QLSKELFAKW VDHPENEIPY PIKDVVLCYG IALGSDKEWD
ILLNTYTNTT NKEEKIQLAY AMSCSKDPWI LNRYMEYAIS TSPFTSNETN IIEVVASSEV
GRYVAKDFLV NNWQAVSKRY GTQSLINLIY TIGRTVTTDL QIVELQQFFS NMLEEHQRIR
VHANLQTIKN ENLKNKKLSA RIAAWLRRNT
