GenomeNet

Database: UniProt
Entry: Q16819
LinkDB: Q16819
Original site: Q16819 
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   13-FEB-2019, entry version 182.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RP   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RP   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
RT   project: 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
RT   human 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:
RT   substrate and inhibitor specificities.";
RL   Biol. Chem. 388:1163-1172(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of protein and peptide substrates
CC         preferentially on carboxyl side of hydrophobic residues.;
CC         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,
CC       the most potent inhibitor is actinonin.
CC       {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
CC       subunits, homooligomer consisting of disulfide-linked alpha
CC       subunit homodimers, or heterotetramer of two alpha and two beta
CC       subunits formed by non-covalent association of two disulfide-
CC       linked heterodimers (By similarity). Interacts with MBL2 through
CC       its carbohydrate moiety. This interaction may inhibit its
CC       catalytic activity (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P14780:MMP9; NbExp=2; IntAct=EBI-8153734, EBI-1382326;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: N-glycosylated; contains GlcNAc, galactose, mannose and a
CC       small amount of fucose. {ECO:0000250}.
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   UniGene; Hs.179704; -.
DR   ProteinModelPortal; Q16819; -.
DR   SMR; Q16819; -.
DR   BioGrid; 110387; 12.
DR   CORUM; Q16819; -.
DR   IntAct; Q16819; 1.
DR   MINT; Q16819; -.
DR   STRING; 9606.ENSP00000230588; -.
DR   MEROPS; M12.002; -.
DR   iPTMnet; Q16819; -.
DR   PhosphoSitePlus; Q16819; -.
DR   BioMuta; MEP1A; -.
DR   DMDM; 205830902; -.
DR   jPOST; Q16819; -.
DR   PaxDb; Q16819; -.
DR   PeptideAtlas; Q16819; -.
DR   PRIDE; Q16819; -.
DR   ProteomicsDB; 61078; -.
DR   Ensembl; ENST00000230588; ENSP00000230588; ENSG00000112818.
DR   GeneID; 4224; -.
DR   KEGG; hsa:4224; -.
DR   UCSC; uc010jzh.2; human.
DR   CTD; 4224; -.
DR   DisGeNET; 4224; -.
DR   EuPathDB; HostDB:ENSG00000112818.9; -.
DR   GeneCards; MEP1A; -.
DR   H-InvDB; HIX0032798; -.
DR   HGNC; HGNC:7015; MEP1A.
DR   HPA; CAB025163; -.
DR   HPA; HPA029416; -.
DR   MIM; 600388; gene.
DR   neXtProt; NX_Q16819; -.
DR   OpenTargets; ENSG00000112818; -.
DR   PharmGKB; PA30749; -.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   GeneTree; ENSGT00940000164139; -.
DR   HOVERGEN; HBG052457; -.
DR   InParanoid; Q16819; -.
DR   KO; K01395; -.
DR   OrthoDB; 241999at2759; -.
DR   PhylomeDB; Q16819; -.
DR   TreeFam; TF315280; -.
DR   BRENDA; 3.4.24.18; 2681.
DR   SignaLink; Q16819; -.
DR   SIGNOR; Q16819; -.
DR   GeneWiki; MEP1A; -.
DR   GenomeRNAi; 4224; -.
DR   PRO; PR:Q16819; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000112818; Expressed in 52 organ(s), highest expression level in jejunal mucosa.
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:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR44155; PTHR44155; 1.
DR   PANTHER; PTHR44155:SF4; PTHR44155:SF4; 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; SSF49599; SSF49599; 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   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Polymorphism;
KW   Protease; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL        1     21       {ECO:0000250}.
FT   PROPEP       22     65       {ECO:0000250}.
FT                                /FTId=PRO_0000028877.
FT   CHAIN        66    746       Meprin A subunit alpha.
FT                                /FTId=PRO_0000028878.
FT   TOPO_DOM     66    712       Extracellular. {ECO:0000255}.
FT   TRANSMEM    713    740       Helical. {ECO:0000255}.
FT   TOPO_DOM    741    746       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       66    260       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      264    433       MAM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN      434    593       MATH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00129}.
FT   DOMAIN      670    710       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   ACT_SITE    156    156       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       155    155       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       159    159       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       165    165       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   CARBOHYD    140    140       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    222    222       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    258    258       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    414    414       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    440    440       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    447    447       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    539    539       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    107    259       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    128    147       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    269    431       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    277    277       Interchain. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DISULFID    308    308       Interchain. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DISULFID    674    685       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    679    694       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    696    709       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VARIANT     469    469       V -> L (in dbSNP:rs2274658).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_020056.
FT   VARIANT     476    476       R -> G (in dbSNP:rs12197930).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_033492.
FT   VARIANT     606    606       T -> S (in dbSNP:rs2297020).
FT                                {ECO:0000269|PubMed:8262185,
FT                                ECO:0000269|Ref.1}.
FT                                /FTId=VAR_051583.
FT   VARIANT     634    634       M -> V (in dbSNP:rs2297019).
FT                                /FTId=VAR_021846.
FT   VARIANT     726    726       T -> M (in dbSNP:rs1804211).
FT                                {ECO:0000269|PubMed:14702039}.
FT                                /FTId=VAR_033493.
FT   CONFLICT     26     26       Y -> H (in Ref. 1; AAA21338).
FT                                {ECO:0000305}.
FT   CONFLICT    162    162       G -> V (in Ref. 2; AAL85339).
FT                                {ECO:0000305}.
FT   CONFLICT    306    306       G -> E (in Ref. 3; BAF98731).
FT                                {ECO:0000305}.
FT   CONFLICT    426    426       L -> P (in Ref. 3; BAF98731).
FT                                {ECO:0000305}.
FT   CONFLICT    518    518       R -> Q (in Ref. 3; BAG37669).
FT                                {ECO:0000305}.
FT   CONFLICT    546    546       R -> S (in Ref. 3; BAF98731).
FT                                {ECO:0000305}.
FT   CONFLICT    638    638       A -> V (in Ref. 3; BAF98731).
FT                                {ECO:0000305}.
FT   CONFLICT    711    713       AVQ -> SAE (in Ref. 1; AAA21338 and 7; no
FT                                nucleotide entry). {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
//
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