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PMGT1_MOUSE
ID   PMGT1_MOUSE             Reviewed;         660 AA.
AC   Q91X88; A2A8F8; Q9D2H7; Q9D5D3; Q9DCN3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1;
DE            Short=POMGnT1;
DE            EC=2.4.1.- {ECO:0000250|UniProtKB:Q8WZA1};
GN   Name=Pomgnt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   STRAIN=129/SvJ;
RA   Minowa M.T., Yoshida A., Endo T., Takeuchi M.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12670716; DOI=10.1016/s0169-328x(03)00055-x;
RA   Henion T.R., Qu Q., Smith F.I.;
RT   "Expression of dystroglycan, fukutin and POMGnT1 during mouse cerebellar
RT   development.";
RL   Brain Res. Mol. Brain Res. 112:177-181(2003).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=26908613; DOI=10.1093/hmg/ddw022;
RA   Xu M., Yamada T., Sun Z., Eblimit A., Lopez I., Wang F., Manya H., Xu S.,
RA   Zhao L., Li Y., Kimchi A., Sharon D., Sui R., Endo T., Koenekoop R.K.,
RA   Chen R.;
RT   "Mutations in POMGNT1 cause non-syndromic retinitis pigmentosa.";
RL   Hum. Mol. Genet. 25:1479-1488(2016).
CC   -!- FUNCTION: Participates in O-mannosyl glycosylation by catalyzing the
CC       addition of N-acetylglucosamine to O-linked mannose on glycoproteins.
CC       Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr
CC       moiety on alpha-dystroglycan and other O-mannosylated proteins,
CC       providing the necessary basis for the addition of further carbohydrate
CC       moieties. Is specific for alpha linked terminal mannose.
CC       {ECO:0000250|UniProtKB:Q8WZA1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + UDP-N-acetyl-
CC         alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-
CC         D-mannosyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54128,
CC         Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:13802, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137323,
CC         ChEBI:CHEBI:138067; Evidence={ECO:0000250|UniProtKB:Q8WZA1};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q8WZA1};
CC       Note=The manganese ion interacts primarily with the substrate UDP-N-
CC       acetylglucosamine. {ECO:0000250|UniProtKB:Q8WZA1};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q8WZA1}.
CC   -!- SUBUNIT: Interacts with DAG1 (via O-linked mannose moiety). Interacts
CC       (via transmembrane domain) with FKTN; the interaction is direct and is
CC       required for normal location in Golgi membranes.
CC       {ECO:0000250|UniProtKB:Q8WZA1}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q8WZA1}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q8WZA1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q91X88-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91X88-2; Sequence=VSP_014972, VSP_014973;
CC       Name=3;
CC         IsoId=Q91X88-3; Sequence=VSP_014974;
CC   -!- TISSUE SPECIFICITY: Expressed at basal body and daughter centriole of
CC       photoreceptor cells (at protein level). {ECO:0000269|PubMed:26908613}.
CC   -!- DEVELOPMENTAL STAGE: Broadly expressed in late embryonic and early
CC       postnatal cerebellar neurons, including premigratory granule neurons of
CC       the external granule cell layer. Expression is maintained in neurons of
CC       the internal granule cell layer after migration is complete. Expressed
CC       in Purkinje cells throughout development. Expressed in Bergmann glial
CC       scaffolds used by granule cells during early posnatal radial migration.
CC       {ECO:0000269|PubMed:12670716}.
CC   -!- DOMAIN: The stem domain mediates specific interaction with beta-linked
CC       N-acetylglucosamine moieties of O-glycosylated proteins. It also
CC       interacts with its product, N-acetyl-beta-D-glucosaminyl-(1->2)-O-
CC       alpha-D-mannosylprotein. {ECO:0000250|UniProtKB:Q8WZA1}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 13 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=POMGnT1;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_594";
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DR   EMBL; AB053220; BAC55021.1; -; mRNA.
DR   EMBL; AB053221; BAC55022.1; -; Genomic_DNA.
DR   EMBL; AK002638; BAB22251.1; -; mRNA.
DR   EMBL; AK019640; BAB31822.1; -; mRNA.
DR   EMBL; AK015478; BAB29863.1; -; mRNA.
DR   EMBL; AL611947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011201; AAH11201.1; -; mRNA.
DR   CCDS; CCDS18506.1; -. [Q91X88-1]
DR   CCDS; CCDS18507.1; -. [Q91X88-3]
DR   CCDS; CCDS71450.1; -. [Q91X88-2]
DR   RefSeq; NP_001277587.1; NM_001290658.1. [Q91X88-2]
DR   RefSeq; NP_080927.1; NM_026651.2. [Q91X88-1]
DR   RefSeq; NP_084062.2; NM_029786.2. [Q91X88-3]
DR   AlphaFoldDB; Q91X88; -.
DR   SMR; Q91X88; -.
DR   BioGRID; 212776; 4.
DR   STRING; 10090.ENSMUSP00000102107; -.
DR   CAZy; GT13; Glycosyltransferase Family 13.
DR   iPTMnet; Q91X88; -.
DR   PhosphoSitePlus; Q91X88; -.
DR   SwissPalm; Q91X88; -.
DR   EPD; Q91X88; -.
DR   jPOST; Q91X88; -.
DR   MaxQB; Q91X88; -.
DR   PaxDb; Q91X88; -.
DR   PeptideAtlas; Q91X88; -.
DR   PRIDE; Q91X88; -.
DR   ProteomicsDB; 289699; -. [Q91X88-1]
DR   ProteomicsDB; 289700; -. [Q91X88-2]
DR   ProteomicsDB; 289701; -. [Q91X88-3]
DR   Antibodypedia; 32757; 109 antibodies from 24 providers.
DR   DNASU; 68273; -.
DR   Ensembl; ENSMUST00000106494; ENSMUSP00000102103; ENSMUSG00000028700. [Q91X88-2]
DR   Ensembl; ENSMUST00000106496; ENSMUSP00000102105; ENSMUSG00000028700. [Q91X88-3]
DR   Ensembl; ENSMUST00000106498; ENSMUSP00000102107; ENSMUSG00000028700. [Q91X88-1]
DR   Ensembl; ENSMUST00000120083; ENSMUSP00000112751; ENSMUSG00000028700. [Q91X88-1]
DR   Ensembl; ENSMUST00000121052; ENSMUSP00000112911; ENSMUSG00000028700. [Q91X88-1]
DR   GeneID; 68273; -.
DR   KEGG; mmu:68273; -.
DR   UCSC; uc008ugh.2; mouse. [Q91X88-1]
DR   UCSC; uc008ugi.2; mouse. [Q91X88-3]
DR   UCSC; uc008ugj.1; mouse. [Q91X88-2]
DR   CTD; 55624; -.
DR   MGI; MGI:1915523; Pomgnt1.
DR   VEuPathDB; HostDB:ENSMUSG00000028700; -.
DR   eggNOG; ENOG502QSG3; Eukaryota.
DR   GeneTree; ENSGT00530000063632; -.
DR   HOGENOM; CLU_024847_0_0_1; -.
DR   InParanoid; Q91X88; -.
DR   OMA; HKKRSWY; -.
DR   OrthoDB; 1324622at2759; -.
DR   PhylomeDB; Q91X88; -.
DR   TreeFam; TF320555; -.
DR   Reactome; R-MMU-5173105; O-linked glycosylation.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 68273; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Pomgnt1; mouse.
DR   PRO; PR:Q91X88; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q91X88; protein.
DR   Bgee; ENSMUSG00000028700; Expressed in lacrimal gland and 268 other tissues.
DR   Genevisible; Q91X88; MM.
DR   GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0008375; F:acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0047223; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; ISO:MGI.
DR   GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR   GO; GO:0016266; P:O-glycan processing; ISS:UniProtKB.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IMP:MGI.
DR   CDD; cd13937; PANDER_GnT-1_2_like; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR004139; Glyco_trans_13.
DR   InterPro; IPR039477; ILEI/PANDER_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR039474; POMGNT1_PANDER-like.
DR   Pfam; PF03071; GNT-I; 1.
DR   Pfam; PF15711; ILEI; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycosyltransferase; Golgi apparatus;
KW   Manganese; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..660
FT                   /note="Protein O-linked-mannose beta-1,2-N-
FT                   acetylglucosaminyltransferase 1"
FT                   /id="PRO_0000191391"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..660
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          68..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..288
FT                   /note="Carbohydrate-binding stem domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   REGION          300..646
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   REGION          473..481
FT                   /note="Interaction with O-glycosylated substrate
FT                   glycoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   REGION          506..512
FT                   /note="Interaction with O-glycosylated substrate
FT                   glycoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   REGION          600..605
FT                   /note="Interaction with O-glycosylated substrate
FT                   glycoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   REGION          634..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         129
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   BINDING         179
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   BINDING         207
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   BINDING         307..311
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   BINDING         338
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   BINDING         371
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   BINDING         394..395
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   BINDING         395
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   BINDING         500
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   BINDING         506..507
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   DISULFID        254..281
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   DISULFID        269..279
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   DISULFID        421..490
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   DISULFID        562..596
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT   VAR_SEQ         1..22
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014972"
FT   VAR_SEQ         23..40
FT                   /note="LTWKYKLTNQRALRRFCQ -> MEGTKEVKDSNGKIQDHG (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014973"
FT   VAR_SEQ         218..250
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014974"
FT   CONFLICT        424
FT                   /note="A -> S (in Ref. 2; BAB29863)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        557
FT                   /note="H -> P (in Ref. 2; BAB22251)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   660 AA;  75110 MW;  4DE09765C0F3EF7C CRC64;
     MDDWKPSPLI KPFGARKKRS WYLTWKYKLT NQRALRRFCQ TGAVLFLLVT VIVNIKLILD
     TRRAISEANE DPEPEQDYDE ALGRLESPRR RGSSPRRVLD VEVYSSRSKV YVAVDGTTVL
     EDEAREQGRG IHVIVLNQAT GHVMAKRVFD TYSPHEDEAM VLFLNMVAPG RVLICTVKDE
     GSFHLKDTAK ALLRSLGSQA GPALGWRDTW AFVGRKGGPV LGEKHSKSPA LSSWGDPVLL
     KTDVPLSSAE EAECHWADTE LNRRRRRFCS KVEGYGSVCS CKDPTPIEFS PDPLPDNKVL
     NVPVAVIAGN RPNYLYRMLR SLLSAQGVSP QMITVFIDGY YEEPMDVVAL FGLRGIQHTP
     ISIKNARVSQ HYKASLTATF NLFPEAKFAV VLEEDLDIAV DFFSFLSQSI HLLEEDDSLY
     CISAWNDQGY EHTAEDPALL YRVETMPGLG WVLRKSLYKE ELEPKWPTPE KLWDWDMWMR
     MPEQRRGREC IIPDVSRSYH FGIVGLNMNG YFHEAYFKKH KFNTVPGVQL RNVDSLKKEA
     YEVEIHRLLS EAEVLDHSKD PCEDSFLPDT EGHTYVAFIR METDDDFATW TQLAKCLHIW
     DLDVRGNHRG LWRLFRKKNH FLVVGVPASP YSVKKPPSVT PIFLEPPPKE EGAPGAAEQT
 
 
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