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MTMR4_HUMAN
ID   MTMR4_HUMAN             Reviewed;        1195 AA.
AC   Q9NYA4; D3DTZ6; Q8IV27; Q9Y4D5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Myotubularin-related protein 4;
DE            EC=3.1.3.48;
DE   AltName: Full=FYVE domain-containing dual specificity protein phosphatase 2;
DE            Short=FYVE-DSP2;
DE   AltName: Full=Zinc finger FYVE domain-containing protein 11;
GN   Name=MTMR4; Synonyms=KIAA0647, ZFYVE11;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANT VAL-170.
RX   PubMed=11302699; DOI=10.1006/excr.2001.5185;
RA   Zhao R., Qi Y., Chen J., Zhao Z.J.;
RT   "FYVE-DSP2, a FYVE domain-containing dual specificity protein phosphatase
RT   that dephosphorylates phosphatidylinositol 3-phosphate.";
RL   Exp. Cell Res. 265:329-338(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-170.
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-280.
RC   TISSUE=Lung;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-610 AND SER-629, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Dephosphorylates proteins phosphorylated on Ser, Thr, and Tyr
CC       residues and low molecular weight phosphatase substrate para-
CC       nitrophenylphosphate. Phosphorylates phosphatidylinositol 3,4,5-
CC       trisphosphate (PIP3). {ECO:0000269|PubMed:11302699}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- INTERACTION:
CC       Q9NYA4; Q15796: SMAD2; NbExp=2; IntAct=EBI-1052346, EBI-1040141;
CC       Q9NYA4; P84022: SMAD3; NbExp=2; IntAct=EBI-1052346, EBI-347161;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11302699}. Membrane
CC       {ECO:0000269|PubMed:11302699}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:11302699}. Note=Localized to perinuclear region.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, spleen, liver,
CC       colon, testis, muscle, placenta, thyroid gland, pancreas, ovary,
CC       prostate, skin, peripheral blood, and bone marrow.
CC       {ECO:0000269|PubMed:11302699}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal brain and fetal liver.
CC       {ECO:0000269|PubMed:11302699}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000305}.
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DR   EMBL; AF264717; AAF72539.1; -; mRNA.
DR   EMBL; AB014547; BAA31622.2; -; mRNA.
DR   EMBL; AC005666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471109; EAW94454.1; -; Genomic_DNA.
DR   EMBL; CH471109; EAW94455.1; -; Genomic_DNA.
DR   EMBL; BC035609; AAH35609.1; -; mRNA.
DR   CCDS; CCDS11608.1; -.
DR   PIR; T00375; T00375.
DR   RefSeq; NP_004678.3; NM_004687.4.
DR   RefSeq; XP_005257843.1; XM_005257786.4.
DR   RefSeq; XP_006722231.1; XM_006722168.3.
DR   AlphaFoldDB; Q9NYA4; -.
DR   SMR; Q9NYA4; -.
DR   BioGRID; 114560; 180.
DR   IntAct; Q9NYA4; 35.
DR   MINT; Q9NYA4; -.
DR   STRING; 9606.ENSP00000325285; -.
DR   DEPOD; MTMR4; -.
DR   GlyGen; Q9NYA4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NYA4; -.
DR   PhosphoSitePlus; Q9NYA4; -.
DR   BioMuta; MTMR4; -.
DR   DMDM; 296438298; -.
DR   EPD; Q9NYA4; -.
DR   jPOST; Q9NYA4; -.
DR   MassIVE; Q9NYA4; -.
DR   MaxQB; Q9NYA4; -.
DR   PaxDb; Q9NYA4; -.
DR   PeptideAtlas; Q9NYA4; -.
DR   PRIDE; Q9NYA4; -.
DR   ProteomicsDB; 83205; -.
DR   Antibodypedia; 30984; 190 antibodies from 26 providers.
DR   DNASU; 9110; -.
DR   Ensembl; ENST00000323456.9; ENSP00000325285.5; ENSG00000108389.10.
DR   GeneID; 9110; -.
DR   KEGG; hsa:9110; -.
DR   UCSC; uc002iwj.3; human.
DR   CTD; 9110; -.
DR   DisGeNET; 9110; -.
DR   GeneCards; MTMR4; -.
DR   HGNC; HGNC:7452; MTMR4.
DR   HPA; ENSG00000108389; Low tissue specificity.
DR   MIM; 603559; gene.
DR   neXtProt; NX_Q9NYA4; -.
DR   OpenTargets; ENSG00000108389; -.
DR   PharmGKB; PA31255; -.
DR   VEuPathDB; HostDB:ENSG00000108389; -.
DR   eggNOG; KOG4471; Eukaryota.
DR   GeneTree; ENSGT00940000158976; -.
DR   HOGENOM; CLU_001839_2_2_1; -.
DR   InParanoid; Q9NYA4; -.
DR   OMA; TRWLQHM; -.
DR   OrthoDB; 824298at2759; -.
DR   PhylomeDB; Q9NYA4; -.
DR   TreeFam; TF315197; -.
DR   PathwayCommons; Q9NYA4; -.
DR   Reactome; R-HSA-1660516; Synthesis of PIPs at the early endosome membrane.
DR   Reactome; R-HSA-1660517; Synthesis of PIPs at the late endosome membrane.
DR   Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR   SignaLink; Q9NYA4; -.
DR   SIGNOR; Q9NYA4; -.
DR   BioGRID-ORCS; 9110; 18 hits in 1079 CRISPR screens.
DR   ChiTaRS; MTMR4; human.
DR   GenomeRNAi; 9110; -.
DR   Pharos; Q9NYA4; Tbio.
DR   PRO; PR:Q9NYA4; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9NYA4; protein.
DR   Bgee; ENSG00000108389; Expressed in middle temporal gyrus and 207 other tissues.
DR   ExpressionAtlas; Q9NYA4; baseline and differential.
DR   Genevisible; Q9NYA4; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:Reactome.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR   GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR   GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:InterPro.
DR   CDD; cd13342; PH-GRAM_MTMR4; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR030590; MTMR4.
DR   InterPro; IPR035997; MTMR4_PH-GRAM.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10807; PTHR10807; 1.
DR   PANTHER; PTHR10807:SF64; PTHR10807:SF64; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Hydrolase; Membrane; Metal-binding; Phosphoprotein;
KW   Protein phosphatase; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..1195
FT                   /note="Myotubularin-related protein 4"
FT                   /id="PRO_0000304809"
FT   DOMAIN          153..570
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT   ZN_FING         1114..1174
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          645..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          827..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1023..1055
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        650..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..854
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        407
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         320..323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         345..346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         407..413
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         453
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         610
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         629
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         170
FT                   /note="L -> V (in dbSNP:rs3744108)"
FT                   /evidence="ECO:0000269|PubMed:11302699,
FT                   ECO:0000269|PubMed:9734811"
FT                   /id="VAR_035110"
FT   VARIANT         280
FT                   /note="S -> G (in dbSNP:rs2302190)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_035111"
FT   VARIANT         297
FT                   /note="V -> G (in dbSNP:rs2302189)"
FT                   /id="VAR_035112"
SQ   SEQUENCE   1195 AA;  133353 MW;  936EC3F69335CEB4 CRC64;
     MGEEGPPSLE YIQAKDLFPP KELVKEEENL QVPFTVLQGE GVEFLGRAAD ALIAISNYRL
     HIKFKDSVIN VPLRMIDSVE SRDMFQLHIS CKDSKVVRCH FSTFKQCQEW LSRLSRATAR
     PAKPEDLFAF AYHAWCLGLT EEDQHTHLCQ PGEHIRCRQE AELARMGFDL QNVWRVSHIN
     SNYKLCPSYP QKLLVPVWIT DKELENVASF RSWKRIPVVV YRHLRNGAAI ARCSQPEISW
     WGWRNADDEY LVTSIAKACA LDPGTRATGG SLSTGNNDTS EACDADFDSS LTACSGVEST
     AAPQKLLILD ARSYTAAVAN RAKGGGCECE EYYPNCEVVF MGMANIHAIR NSFQYLRAVC
     SQMPDPSNWL SALESTKWLQ HLSVMLKAAV LVANTVDREG RPVLVHCSDG WDRTPQIVAL
     AKILLDPYYR TLEGFQVLVE SDWLDFGHKF GDRCGHQENV EDQNEQCPVF LQWLDSVHQL
     LKQFPCLFEF NEAFLVKLVQ HTYSCLYGTF LANNPCEREK RNIYKRTCSV WALLRAGNKN
     FHNFLYTPSS DMVLHPVCHV RALHLWTAVY LPASSPCTLG EENMDLYLSP VAQSQEFSGR
     SLDRLPKTRS MDDLLSACDT SSPLTRTSSD PNLNNHCQEV RVGLEPWHSN PEGSETSFVD
     SGVGGPQQTV GEVGLPPPLP SSQKDYLSNK PFKSHKSCSP SYKLLNTAVP REMKSNTSDP
     EIKVLEETKG PAPDPSAQDE LGRTLDGIGE PPEHCPETEA VSALSKVISN KCDGVCNFPE
     SSQNSPTGTP QQAQPDSMLG VPSKCVLDHS LSTVCNPPSA ACQTPLDPST DFLNQDPSGS
     VASISHQEQL SSVPDLTHGE EDIGKRGNNR NGQLLENPRF GKMPLELVRK PISQSQISEF
     SFLGSNWDSF QGMVTSFPSG EATPRRLLSY GCCSKRPNSK QMRATGPCFG GQWAQREGVK
     SPVCSSHSNG HCTGPGGKNQ MWLSSHPKQV SSTKPVPLNC PSPVPPLYLD DDGLPFPTDV
     IQHRLRQIEA GYKQEVEQLR RQVRELQMRL DIRHCCAPPA EPPMDYEDDF TCLKESDGSD
     TEDFGSDHSE DCLSEASWEP VDKKETEVTR WVPDHMASHC YNCDCEFWLA KRRHHCRNCG
     NVFCAGCCHL KLPIPDQQLY DPVLVCNSCY EHIQVSRARE LMSQQLKKPI ATASS
 
 
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