MEP1A_HUMAN
ID MEP1A_HUMAN Reviewed; 746 AA.
AC Q16819; A2RRM4; B0AZP9; B2RCS2; Q8TDC9; Q9H1R1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Meprin A subunit alpha;
DE EC=3.4.24.18;
DE AltName: Full=Endopeptidase-2;
DE AltName: Full=N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit alpha;
DE AltName: Full=PABA peptide hydrolase;
DE AltName: Full=PPH alpha;
DE Flags: Precursor;
GN Name=MEP1A;
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], AND VARIANT SER-606.
RC TISSUE=Jejunum;
RA Sterchi E.E.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Small intestine;
RA Haun R.S.;
RT "Expression of human meprin alpha.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-469 AND MET-726.
RC TISSUE=Colon, and Small intestine;
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-469 AND GLY-476.
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-746, AND VARIANT SER-606.
RC TISSUE=Jejunum;
RX PubMed=8262185; DOI=10.1016/0014-5793(93)80421-p;
RA Dumermuth E., Eldering J.A., Gruenberg J., Jiang W., Sterchi E.E.;
RT "Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human
RT small intestine and its expression in COS-1 cells.";
RL FEBS Lett. 335:367-375(1993).
RN [8]
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17976009; DOI=10.1515/bc.2007.156;
RA Bylander J.E., Bertenshaw G.P., Matters G.L., Hubbard S.J., Bond J.S.;
RT "Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate
RT and inhibitor specificities.";
RL Biol. Chem. 388:1163-1172(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of protein and peptide substrates preferentially on
CC carboxyl side of hydrophobic residues.; EC=3.4.24.18;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211};
CC -!- ACTIVITY REGULATION: Inhibited by several hydroxamate compounds, the
CC most potent inhibitor is actinonin. {ECO:0000269|PubMed:17976009}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 uM for GRP {ECO:0000269|PubMed:17976009};
CC KM=18.0 uM for PTH 12-34 {ECO:0000269|PubMed:17976009};
CC KM=33.9 uM for secretin {ECO:0000269|PubMed:17976009};
CC KM=41.3 uM for substance P {ECO:0000269|PubMed:17976009};
CC KM=56.5 uM for LHRH {ECO:0000269|PubMed:17976009};
CC KM=73.2 uM for orcokinin {ECO:0000269|PubMed:17976009};
CC KM=292 uM for alpha-MSH {ECO:0000269|PubMed:17976009};
CC KM=125 uM for bradykinin {ECO:0000269|PubMed:17976009};
CC KM=200 uM for gastrin {ECO:0000269|PubMed:17976009};
CC -!- SUBUNIT: Homotetramer consisting of disulfide-linked alpha subunits,
CC homooligomer consisting of disulfide-linked alpha subunit homodimers,
CC or heterotetramer of two alpha and two beta subunits formed by non-
CC covalent association of two disulfide-linked heterodimers (By
CC similarity). Interacts with MBL2 through its carbohydrate moiety. This
CC interaction may inhibit its catalytic activity (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q16819; P14780: MMP9; NbExp=2; IntAct=EBI-8153734, EBI-1382326;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- PTM: N-glycosylated; contains GlcNAc, galactose, mannose and a small
CC amount of fucose. {ECO:0000250}.
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DR EMBL; M82962; AAA21338.1; -; mRNA.
DR EMBL; AF478685; AAL85339.1; -; mRNA.
DR EMBL; AK290282; BAF82971.1; -; mRNA.
DR EMBL; AK315246; BAG37669.1; -; mRNA.
DR EMBL; AK315840; BAF98731.1; -; mRNA.
DR EMBL; AL161618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04306.1; -; Genomic_DNA.
DR EMBL; BC131714; AAI31715.1; -; mRNA.
DR CCDS; CCDS4918.1; -.
DR PIR; S60193; HYHUMA.
DR RefSeq; NP_005579.2; NM_005588.2.
DR AlphaFoldDB; Q16819; -.
DR SMR; Q16819; -.
DR BioGRID; 110387; 12.
DR CORUM; Q16819; -.
DR IntAct; Q16819; 1.
DR MINT; Q16819; -.
DR STRING; 9606.ENSP00000230588; -.
DR BindingDB; Q16819; -.
DR ChEMBL; CHEMBL4105775; -.
DR MEROPS; M12.002; -.
DR GlyGen; Q16819; 8 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q16819; -.
DR PhosphoSitePlus; Q16819; -.
DR BioMuta; MEP1A; -.
DR DMDM; 205830902; -.
DR jPOST; Q16819; -.
DR MassIVE; Q16819; -.
DR PaxDb; Q16819; -.
DR PeptideAtlas; Q16819; -.
DR PRIDE; Q16819; -.
DR ProteomicsDB; 61078; -.
DR Antibodypedia; 30753; 265 antibodies from 31 providers.
DR DNASU; 4224; -.
DR Ensembl; ENST00000230588.9; ENSP00000230588.4; ENSG00000112818.11.
DR GeneID; 4224; -.
DR KEGG; hsa:4224; -.
DR MANE-Select; ENST00000230588.9; ENSP00000230588.4; NM_005588.3; NP_005579.2.
DR UCSC; uc010jzh.2; human.
DR CTD; 4224; -.
DR DisGeNET; 4224; -.
DR GeneCards; MEP1A; -.
DR HGNC; HGNC:7015; MEP1A.
DR HPA; ENSG00000112818; Tissue enriched (intestine).
DR MIM; 600388; gene.
DR neXtProt; NX_Q16819; -.
DR OpenTargets; ENSG00000112818; -.
DR PharmGKB; PA30749; -.
DR VEuPathDB; HostDB:ENSG00000112818; -.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000164139; -.
DR InParanoid; Q16819; -.
DR OMA; FEMFRLR; -.
DR PhylomeDB; Q16819; -.
DR TreeFam; TF315280; -.
DR BRENDA; 3.4.24.18; 2681.
DR PathwayCommons; Q16819; -.
DR SignaLink; Q16819; -.
DR SIGNOR; Q16819; -.
DR BioGRID-ORCS; 4224; 16 hits in 1070 CRISPR screens.
DR GeneWiki; MEP1A; -.
DR GenomeRNAi; 4224; -.
DR Pharos; Q16819; Tchem.
DR PRO; PR:Q16819; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q16819; protein.
DR Bgee; ENSG00000112818; Expressed in ileal mucosa and 69 other tissues.
DR ExpressionAtlas; Q16819; baseline and differential.
DR Genevisible; Q16819; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0017090; C:meprin A complex; IDA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0070573; F:metallodipeptidase activity; IDA:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0038004; P:epidermal growth factor receptor ligand maturation; IDA:MGI.
DR GO; GO:0140448; P:signaling receptor ligand precursor processing; IDA:MGI.
DR CDD; cd06263; MAM; 1.
DR CDD; cd04282; ZnMc_meprin; 1.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR008294; Meprin.
DR InterPro; IPR034301; Meprin_alpha.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR034038; ZnMP_meprin.
DR PANTHER; PTHR10127:SF824; PTHR10127:SF824; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00629; MAM; 1.
DR PIRSF; PIRSF001196; Meprin; 1.
DR PRINTS; PR00480; ASTACIN.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00061; MATH; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT PROPEP 22..65
FT /evidence="ECO:0000250"
FT /id="PRO_0000028877"
FT CHAIN 66..746
FT /note="Meprin A subunit alpha"
FT /id="PRO_0000028878"
FT TOPO_DOM 66..712
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..746
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 66..260
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 264..433
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 434..593
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 670..710
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 642..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 128..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 269..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 277
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 308
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 674..685
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 679..694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 696..709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VARIANT 469
FT /note="V -> L (in dbSNP:rs2274658)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_020056"
FT VARIANT 476
FT /note="R -> G (in dbSNP:rs12197930)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033492"
FT VARIANT 606
FT /note="T -> S (in dbSNP:rs2297020)"
FT /evidence="ECO:0000269|PubMed:8262185, ECO:0000269|Ref.1"
FT /id="VAR_051583"
FT VARIANT 634
FT /note="M -> V (in dbSNP:rs2297019)"
FT /id="VAR_021846"
FT VARIANT 726
FT /note="T -> M (in dbSNP:rs1804211)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_033493"
FT CONFLICT 26
FT /note="Y -> H (in Ref. 1; AAA21338)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="G -> V (in Ref. 2; AAL85339)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="G -> E (in Ref. 3; BAF98731)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="L -> P (in Ref. 3; BAF98731)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="R -> Q (in Ref. 3; BAG37669)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="R -> S (in Ref. 3; BAF98731)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="A -> V (in Ref. 3; BAF98731)"
FT /evidence="ECO:0000305"
FT CONFLICT 711..713
FT /note="AVQ -> SAE (in Ref. 1; AAA21338 and 7; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 84419 MW; B5F0812F2850F958 CRC64;
MAWIRSTCIL FFTLLFAHIA AVPIKYLPEE NVHDADFGEQ KDISEINLAA GLDLFQGDIL
LQKSRNGLRD PNTRWTFPIP YILADNLGLN AKGAILYAFE MFRLKSCVDF KPYEGESSYI
IFQQFDGCWS EVGDQHVGQN ISIGQGCAYK AIIEHEILHA LGFYHEQSRT DRDDYVNIWW
DQILSGYQHN FDTYDDSLIT DLNTPYDYES LMHYQPFSFN KNASVPTITA KIPEFNSIIG
QRLDFSAIDL ERLNRMYNCT TTHTLLDHCT FEKANICGMI QGTRDDTDWA HQDSAQAGEV
DHTLLGQCTG AGYFMQFSTS SGSAEEAALL ESRILYPKRK QQCLQFFYKM TGSPSDRLVV
WVRRDDSTGN VRKLVKVQTF QGDDDHNWKI AHVVLKEEQK FRYLFQGTKG DPQNSTGGIY
LDDITLTETP CPTGVWTVRN FSQVLENTSK GDKLQSPRFY NSEGYGFGVT LYPNSRESSG
YLRLAFHVCS GENDAILEWP VENRQVIITI LDQEPDVRNR MSSSMVFTTS KSHTSPAIND
TVIWDRPSRV GTYHTDCNCF RSIDLGWSGF ISHQMLKRRS FLKNDDLIIF VDFEDITHLS
QTEVPTKGKR LSPQGLILQG QEQQVSEEGS GKAMLEEALP VSLSQGQPSR QKRSVENTGP
LEDHNWPQYF RDPCDPNPCQ NDGICVNVKG MASCRCISGH AFFYTGERCQ AVQVHGSVLG
MVIGGTAGVI FLTFSIIAIL SQRPRK
