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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
 
 
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