ERMP1_HUMAN
ID ERMP1_HUMAN Reviewed; 904 AA.
AC Q7Z2K6; B2RNA4; B3KSB1; Q8N5T5; Q9H5M1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Endoplasmic reticulum metallopeptidase 1 {ECO:0000250|UniProtKB:Q6UPR8, ECO:0000312|HGNC:HGNC:23703};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=Felix-ina {ECO:0000250|UniProtKB:Q6UPR8};
GN Name=ERMP1 {ECO:0000312|HGNC:HGNC:23703};
GN Synonyms=FXNA {ECO:0000250|UniProtKB:Q6UPR8},
GN KIAA1815 {ECO:0000303|PubMed:11347906};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hepatoma, Hippocampus, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-904 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [5]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-730.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Within the ovary, required for the organization of somatic
CC cells and oocytes into discrete follicular structures.
CC {ECO:0000250|UniProtKB:Q6UPR8}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- INTERACTION:
CC Q7Z2K6; P41181: AQP2; NbExp=3; IntAct=EBI-10976398, EBI-12701138;
CC Q7Z2K6; Q13520: AQP6; NbExp=3; IntAct=EBI-10976398, EBI-13059134;
CC Q7Z2K6; Q9UN42: ATP1B4; NbExp=3; IntAct=EBI-10976398, EBI-12894731;
CC Q7Z2K6; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-10976398, EBI-747430;
CC Q7Z2K6; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-10976398, EBI-11532900;
CC Q7Z2K6; Q8TD46-4: CD200R1; NbExp=3; IntAct=EBI-10976398, EBI-12824513;
CC Q7Z2K6; O00501: CLDN5; NbExp=3; IntAct=EBI-10976398, EBI-18400628;
CC Q7Z2K6; O95471: CLDN7; NbExp=3; IntAct=EBI-10976398, EBI-740744;
CC Q7Z2K6; O95484: CLDN9; NbExp=3; IntAct=EBI-10976398, EBI-18341636;
CC Q7Z2K6; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-10976398, EBI-11749983;
CC Q7Z2K6; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-10976398, EBI-6942903;
CC Q7Z2K6; P60508: ERVFRD-1; NbExp=3; IntAct=EBI-10976398, EBI-17973325;
CC Q7Z2K6; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10976398, EBI-18304435;
CC Q7Z2K6; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-10976398, EBI-12142257;
CC Q7Z2K6; P48165: GJA8; NbExp=3; IntAct=EBI-10976398, EBI-17458373;
CC Q7Z2K6; O15529: GPR42; NbExp=3; IntAct=EBI-10976398, EBI-18076404;
CC Q7Z2K6; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-10976398, EBI-13067820;
CC Q7Z2K6; Q9UM44: HHLA2; NbExp=3; IntAct=EBI-10976398, EBI-2867874;
CC Q7Z2K6; P31937: HIBADH; NbExp=3; IntAct=EBI-10976398, EBI-11427100;
CC Q7Z2K6; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-10976398, EBI-725665;
CC Q7Z2K6; P38484: IFNGR2; NbExp=3; IntAct=EBI-10976398, EBI-3905457;
CC Q7Z2K6; Q9UGI6-2: KCNN3; NbExp=3; IntAct=EBI-10976398, EBI-17888181;
CC Q7Z2K6; P26715: KLRC1; NbExp=3; IntAct=EBI-10976398, EBI-9018187;
CC Q7Z2K6; Q6UWN5: LYPD5; NbExp=3; IntAct=EBI-10976398, EBI-17200970;
CC Q7Z2K6; Q95460-2: MR1; NbExp=3; IntAct=EBI-10976398, EBI-12201447;
CC Q7Z2K6; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-10976398, EBI-16427978;
CC Q7Z2K6; O00623: PEX12; NbExp=3; IntAct=EBI-10976398, EBI-594836;
CC Q7Z2K6; Q9UBD6: RHCG; NbExp=3; IntAct=EBI-10976398, EBI-15853497;
CC Q7Z2K6; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-10976398, EBI-12808018;
CC Q7Z2K6; A1A5C7-2: SLC22A23; NbExp=3; IntAct=EBI-10976398, EBI-12081840;
CC Q7Z2K6; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-10976398, EBI-5235586;
CC Q7Z2K6; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-10976398, EBI-10819434;
CC Q7Z2K6; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-10976398, EBI-17280858;
CC Q7Z2K6; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-10976398, EBI-10982110;
CC Q7Z2K6; Q9NWC5: TMEM45A; NbExp=3; IntAct=EBI-10976398, EBI-10823938;
CC Q7Z2K6; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-10976398, EBI-11742770;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6UPR8}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z2K6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z2K6-2; Sequence=VSP_056121, VSP_056122;
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15604.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK026962; BAB15604.1; ALT_INIT; mRNA.
DR EMBL; AK093217; BAG52673.1; -; mRNA.
DR EMBL; AK127218; BAG54455.1; -; mRNA.
DR EMBL; AL136980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031630; AAH31630.2; -; mRNA.
DR EMBL; BC136771; AAI36772.1; -; mRNA.
DR EMBL; BC136773; AAI36774.1; -; mRNA.
DR EMBL; AB058718; BAB47444.2; -; mRNA.
DR CCDS; CCDS34983.1; -. [Q7Z2K6-1]
DR RefSeq; NP_079172.2; NM_024896.2. [Q7Z2K6-1]
DR AlphaFoldDB; Q7Z2K6; -.
DR SMR; Q7Z2K6; -.
DR BioGRID; 123025; 179.
DR IntAct; Q7Z2K6; 63.
DR MINT; Q7Z2K6; -.
DR STRING; 9606.ENSP00000340427; -.
DR MEROPS; M28.018; -.
DR GlyConnect; 1205; 2 N-Linked glycans (1 site).
DR GlyGen; Q7Z2K6; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q7Z2K6; -.
DR PhosphoSitePlus; Q7Z2K6; -.
DR SwissPalm; Q7Z2K6; -.
DR BioMuta; ERMP1; -.
DR DMDM; 117949602; -.
DR EPD; Q7Z2K6; -.
DR jPOST; Q7Z2K6; -.
DR MassIVE; Q7Z2K6; -.
DR MaxQB; Q7Z2K6; -.
DR PaxDb; Q7Z2K6; -.
DR PeptideAtlas; Q7Z2K6; -.
DR PRIDE; Q7Z2K6; -.
DR ProteomicsDB; 3630; -.
DR ProteomicsDB; 68961; -. [Q7Z2K6-1]
DR ABCD; Q7Z2K6; 5 sequenced antibodies.
DR Antibodypedia; 54615; 157 antibodies from 24 providers.
DR DNASU; 79956; -.
DR Ensembl; ENST00000339450.10; ENSP00000340427.5; ENSG00000099219.15. [Q7Z2K6-1]
DR Ensembl; ENST00000462592.5; ENSP00000417160.1; ENSG00000099219.15. [Q7Z2K6-1]
DR Ensembl; ENST00000487088.6; ENSP00000432986.2; ENSG00000099219.15. [Q7Z2K6-1]
DR Ensembl; ENST00000688202.1; ENSP00000510190.1; ENSG00000099219.15. [Q7Z2K6-1]
DR Ensembl; ENST00000689268.1; ENSP00000509900.1; ENSG00000099219.15. [Q7Z2K6-1]
DR Ensembl; ENST00000689364.1; ENSP00000509092.1; ENSG00000099219.15. [Q7Z2K6-1]
DR Ensembl; ENST00000690284.1; ENSP00000509328.1; ENSG00000099219.15. [Q7Z2K6-1]
DR GeneID; 79956; -.
DR KEGG; hsa:79956; -.
DR MANE-Select; ENST00000339450.10; ENSP00000340427.5; NM_024896.3; NP_079172.2.
DR UCSC; uc003zjm.2; human. [Q7Z2K6-1]
DR CTD; 79956; -.
DR DisGeNET; 79956; -.
DR GeneCards; ERMP1; -.
DR HGNC; HGNC:23703; ERMP1.
DR HPA; ENSG00000099219; Tissue enhanced (parathyroid).
DR MalaCards; ERMP1; -.
DR MIM; 611156; gene.
DR neXtProt; NX_Q7Z2K6; -.
DR OpenTargets; ENSG00000099219; -.
DR PharmGKB; PA162385366; -.
DR VEuPathDB; HostDB:ENSG00000099219; -.
DR eggNOG; KOG2194; Eukaryota.
DR GeneTree; ENSGT00530000063839; -.
DR HOGENOM; CLU_007536_2_0_1; -.
DR InParanoid; Q7Z2K6; -.
DR OMA; WNNTIGA; -.
DR PhylomeDB; Q7Z2K6; -.
DR TreeFam; TF314836; -.
DR PathwayCommons; Q7Z2K6; -.
DR SignaLink; Q7Z2K6; -.
DR SIGNOR; Q7Z2K6; -.
DR BioGRID-ORCS; 79956; 13 hits in 1083 CRISPR screens.
DR ChiTaRS; ERMP1; human.
DR GenomeRNAi; 79956; -.
DR Pharos; Q7Z2K6; Tbio.
DR PRO; PR:Q7Z2K6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q7Z2K6; protein.
DR Bgee; ENSG00000099219; Expressed in palpebral conjunctiva and 204 other tissues.
DR ExpressionAtlas; Q7Z2K6; baseline and differential.
DR Genevisible; Q7Z2K6; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:FlyBase.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:FlyBase.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..904
FT /note="Endoplasmic reticulum metallopeptidase 1"
FT /id="PRO_0000259492"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..399
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 400..420
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 458..478
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..489
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 490..510
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 520..540
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 542..562
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 580..600
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 601..621
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 622..642
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 652..672
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..904
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 251
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 353
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 204..222
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056121"
FT VAR_SEQ 576..904
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056122"
FT VARIANT 44
FT /note="S -> N (in dbSNP:rs13284203)"
FT /id="VAR_028945"
FT CONFLICT 575
FT /note="G -> D (in Ref. 1; BAG52673)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="E -> A (in Ref. 1; BAB15604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 100231 MW; 3A723027C53092EF CRC64;
MEWGSESAAV RRHRVGVERR EGAAAAPPPE REARAQEPLV DGCSGGGRTR KRSPGGSGGA
SRGAGTGLSE VRAALGLALY LIALRTLVQL SLQQLVLRGA AGHRGEFDAL QARDYLEHIT
SIGPRTTGSP ENEILTVHYL LEQIKLIEVQ SNSLHKISVD VQRPTGSFSI DFLGGFTSYY
DNITNVVVKL EPRDGAQHAV LANCHFDSVA NSPGASDDAV SCSVMLEVLR VLSTSSEALH
HAVIFLFNGA EENVLQASHG FITQHPWASL IRAFINLEAA GVGGKELVFQ TGPENPWLVQ
AYVSAAKHPF ASVVAQEVFQ SGIIPSDTDF RIYRDFGNIP GIDLAFIENG YIYHTKYDTA
DRILTDSIQR AGDNILAVLK HLATSDMLAA ASKYRHGNMV FFDVLGLFVI AYPSRIGSII
NYMVVMGVVL YLGKKFLQPK HKTGNYKKDF LCGLGITLIS WFTSLVTVLI IAVFISLIGQ
SLSWYNHFYV SVCLYGTATV AKIILIHTLA KRFYYMNASA QYLGEVFFDI SLFVHCCFLV
TLTYQGLCSA FISAVWVAFP LLTKLCVHKD FKQHGAQGKF IAFYLLGMFI PYLYALYLIW
AVFEMFTPIL GRSGSEIPPD VVLASILAGC TMILSSYFIN FIYLAKSTKK TMLTLTLVCA
ITFLLVCSGT FFPYSSNPAN PKPKRVFLQH MTRTFHDLEG NAVKRDSGIW INGFDYTGIS
HITPHIPEIN DSIRAHCEEN APLCGFPWYL PVHFLIRKNW YLPAPEVSPR NPPHFRLISK
EQTPWDSIKL TFEATGPSHM SFYVRAHKGS TLSQWSLGNG TPVTSKGGDY FVFYSHGLQA
SAWQFWIEVQ VSEEHPEGMV TVAIAAHYLS GEDKRSPQLD ALKEKFPDWT FPSAWVCTYD
LFVF
