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LRP12_HUMAN
ID   LRP12_HUMAN             Reviewed;         859 AA.
AC   Q9Y561; A8K137; B4DRQ2;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=Low-density lipoprotein receptor-related protein 12;
DE            Short=LDLR-related protein 12;
DE            Short=LRP-12;
DE   AltName: Full=Suppressor of tumorigenicity 7 protein;
DE   Flags: Precursor;
GN   Name=LRP12; Synonyms=ST7;
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 {ECO:0000312|EMBL:AAD44360.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=9927190; DOI=10.1038/sj.onc.1202290;
RA   Qing J., Wei D., Maher V.M., McCormick J.J.;
RT   "Cloning and characterization of a novel gene encoding a putative
RT   transmembrane protein with altered expression in some human transformed and
RT   tumor-derived cell lines.";
RL   Oncogene 18:335-342(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4] {ECO:0000305}
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Retinal pigment epithelium;
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   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND POSSIBLE INTERACTION WITH RACK1; ZFYVE9
RP   AND NMRK2.
RX   PubMed=12809483; DOI=10.1021/bi034081y;
RA   Battle M.A., Maher V.M., McCormick J.J.;
RT   "ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with
RT   a cytoplasmic tail that interacts with proteins related to signal
RT   transduction pathways.";
RL   Biochemistry 42:7270-7282(2003).
RN   [7]
RP   INVOLVEMENT IN OPDM1.
RX   PubMed=31332380; DOI=10.1038/s41588-019-0458-z;
RA   Ishiura H., Shibata S., Yoshimura J., Suzuki Y., Qu W., Doi K.,
RA   Almansour M.A., Kikuchi J.K., Taira M., Mitsui J., Takahashi Y.,
RA   Ichikawa Y., Mano T., Iwata A., Harigaya Y., Matsukawa M.K., Matsukawa T.,
RA   Tanaka M., Shirota Y., Ohtomo R., Kowa H., Date H., Mitsue A., Hatsuta H.,
RA   Morimoto S., Murayama S., Shiio Y., Saito Y., Mitsutake A., Kawai M.,
RA   Sasaki T., Sugiyama Y., Hamada M., Ohtomo G., Terao Y., Nakazato Y.,
RA   Takeda A., Sakiyama Y., Umeda-Kameyama Y., Shinmi J., Ogata K., Kohno Y.,
RA   Lim S.Y., Tan A.H., Shimizu J., Goto J., Nishino I., Toda T., Morishita S.,
RA   Tsuji S.;
RT   "Noncoding CGG repeat expansions in neuronal intranuclear inclusion
RT   disease, oculopharyngodistal myopathy and an overlapping disease.";
RL   Nat. Genet. 51:1222-1232(2019).
CC   -!- FUNCTION: Probable receptor, which may be involved in the
CC       internalization of lipophilic molecules and/or signal transduction. May
CC       act as a tumor suppressor. {ECO:0000269|PubMed:12809483}.
CC   -!- SUBUNIT: May interact with RACK1, ZFYVE9 and NMRK2.
CC   -!- INTERACTION:
CC       Q9Y561; Q9NPI5: NMRK2; NbExp=2; IntAct=EBI-296693, EBI-514059;
CC       Q9Y561; P63244: RACK1; NbExp=2; IntAct=EBI-296693, EBI-296739;
CC       Q9Y561; O95405: ZFYVE9; NbExp=2; IntAct=EBI-296693, EBI-296817;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12809483}; Single-
CC       pass type I membrane protein {ECO:0000269|PubMed:12809483}. Membrane,
CC       coated pit {ECO:0000269|PubMed:12809483}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y561-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y561-2; Sequence=VSP_040992;
CC   -!- TISSUE SPECIFICITY: Widely expressed in heart, skeletal muscle, brain,
CC       lung, placenta and pancreas, but not in tissues consisting of a large
CC       number of epithelial cells, such as liver and kidney. Expressed at very
CC       low levels in a number of tumor-derived cell lines.
CC       {ECO:0000269|PubMed:9927190}.
CC   -!- DISEASE: Oculopharyngodistal myopathy 1 (OPDM1) [MIM:164310]: A form of
CC       oculopharyngodistal myopathy, a muscle disorder characterized by
CC       progressive ptosis, external ophthalmoplegia, and weakness of the
CC       masseter, facial, pharyngeal, and distal limb muscles. The
CC       myopathological features are presence of rimmed vacuoles in the muscle
CC       fibers and myopathic changes of differing severity. OPDM1 inheritance
CC       pattern is autosomal dominant. {ECO:0000269|PubMed:31332380}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry. The causative mutation is a heterozygous trinucleotide repeat
CC       expansion (CGG) in the 5-prime untranslated region of the gene.
CC       {ECO:0000269|PubMed:31332380}.
CC   -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR   EMBL; AF166350; AAD44360.1; -; mRNA.
DR   EMBL; AK289752; BAF82441.1; -; mRNA.
DR   EMBL; AK299374; BAG61364.1; -; mRNA.
DR   EMBL; AC087370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471060; EAW91897.1; -; Genomic_DNA.
DR   EMBL; BC032109; AAH32109.1; -; mRNA.
DR   CCDS; CCDS47907.1; -. [Q9Y561-2]
DR   CCDS; CCDS6303.1; -. [Q9Y561-1]
DR   RefSeq; NP_001129175.1; NM_001135703.2. [Q9Y561-2]
DR   RefSeq; NP_038465.1; NM_013437.4. [Q9Y561-1]
DR   AlphaFoldDB; Q9Y561; -.
DR   BioGRID; 119000; 51.
DR   IntAct; Q9Y561; 29.
DR   MINT; Q9Y561; -.
DR   STRING; 9606.ENSP00000276654; -.
DR   GlyGen; Q9Y561; 6 sites.
DR   iPTMnet; Q9Y561; -.
DR   PhosphoSitePlus; Q9Y561; -.
DR   SwissPalm; Q9Y561; -.
DR   BioMuta; LRP12; -.
DR   DMDM; 25091287; -.
DR   EPD; Q9Y561; -.
DR   jPOST; Q9Y561; -.
DR   MassIVE; Q9Y561; -.
DR   MaxQB; Q9Y561; -.
DR   PaxDb; Q9Y561; -.
DR   PeptideAtlas; Q9Y561; -.
DR   PRIDE; Q9Y561; -.
DR   ProteomicsDB; 86291; -. [Q9Y561-1]
DR   ProteomicsDB; 86292; -. [Q9Y561-2]
DR   Antibodypedia; 2508; 192 antibodies from 31 providers.
DR   DNASU; 29967; -.
DR   Ensembl; ENST00000276654.10; ENSP00000276654.5; ENSG00000147650.12. [Q9Y561-1]
DR   Ensembl; ENST00000424843.6; ENSP00000399148.2; ENSG00000147650.12. [Q9Y561-2]
DR   GeneID; 29967; -.
DR   KEGG; hsa:29967; -.
DR   MANE-Select; ENST00000276654.10; ENSP00000276654.5; NM_013437.5; NP_038465.1.
DR   UCSC; uc003yma.4; human. [Q9Y561-1]
DR   CTD; 29967; -.
DR   DisGeNET; 29967; -.
DR   GeneCards; LRP12; -.
DR   HGNC; HGNC:31708; LRP12.
DR   HPA; ENSG00000147650; Low tissue specificity.
DR   MalaCards; LRP12; -.
DR   MIM; 164310; phenotype.
DR   MIM; 618299; gene.
DR   neXtProt; NX_Q9Y561; -.
DR   OpenTargets; ENSG00000147650; -.
DR   PharmGKB; PA134921850; -.
DR   VEuPathDB; HostDB:ENSG00000147650; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   GeneTree; ENSGT00940000158307; -.
DR   InParanoid; Q9Y561; -.
DR   OMA; DQFHCGN; -.
DR   PhylomeDB; Q9Y561; -.
DR   TreeFam; TF332149; -.
DR   PathwayCommons; Q9Y561; -.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   SignaLink; Q9Y561; -.
DR   BioGRID-ORCS; 29967; 11 hits in 1081 CRISPR screens.
DR   ChiTaRS; LRP12; human.
DR   GenomeRNAi; 29967; -.
DR   Pharos; Q9Y561; Tbio.
DR   PRO; PR:Q9Y561; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9Y561; protein.
DR   Bgee; ENSG00000147650; Expressed in stromal cell of endometrium and 173 other tissues.
DR   ExpressionAtlas; Q9Y561; baseline and differential.
DR   Genevisible; Q9Y561; HS.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; NAS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR   GO; GO:0040011; P:locomotion; IBA:GO_Central.
DR   GO; GO:0001764; P:neuron migration; IDA:MGI.
DR   GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR   GO; GO:0040008; P:regulation of growth; NAS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00112; LDLa; 5.
DR   Gene3D; 2.60.120.290; -; 2.
DR   Gene3D; 4.10.400.10; -; 5.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00057; Ldl_recept_a; 4.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00192; LDLa; 5.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF57424; SSF57424; 5.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coated pit; Disulfide bond; Endocytosis;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..859
FT                   /note="Low-density lipoprotein receptor-related protein 12"
FT                   /id="PRO_0000017339"
FT   TOPO_DOM        33..492
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        514..859
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..159
FT                   /note="CUB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          165..201
FT                   /note="LDL-receptor class A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          214..255
FT                   /note="LDL-receptor class A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          259..372
FT                   /note="CUB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          374..411
FT                   /note="LDL-receptor class A 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          412..449
FT                   /note="LDL-receptor class A 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          450..486
FT                   /note="LDL-receptor class A 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   REGION          623..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..663
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..76
FT                   /evidence="ECO:0000250"
FT   DISULFID        103..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        166..178
FT                   /evidence="ECO:0000250"
FT   DISULFID        173..191
FT                   /evidence="ECO:0000250"
FT   DISULFID        185..200
FT                   /evidence="ECO:0000250"
FT   DISULFID        215..232
FT                   /evidence="ECO:0000250"
FT   DISULFID        222..245
FT                   /evidence="ECO:0000250"
FT   DISULFID        239..254
FT                   /evidence="ECO:0000250"
FT   DISULFID        259..285
FT                   /evidence="ECO:0000250"
FT   DISULFID        375..388
FT                   /evidence="ECO:0000250"
FT   DISULFID        382..401
FT                   /evidence="ECO:0000250"
FT   DISULFID        395..410
FT                   /evidence="ECO:0000250"
FT   DISULFID        413..426
FT                   /evidence="ECO:0000250"
FT   DISULFID        420..439
FT                   /evidence="ECO:0000250"
FT   DISULFID        433..448
FT                   /evidence="ECO:0000250"
FT   DISULFID        451..463
FT                   /evidence="ECO:0000250"
FT   DISULFID        458..476
FT                   /evidence="ECO:0000250"
FT   DISULFID        470..485
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         27..45
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040992"
FT   VARIANT         694
FT                   /note="S -> G (in dbSNP:rs16871494)"
FT                   /id="VAR_049766"
SQ   SEQUENCE   859 AA;  94984 MW;  41A8FD8121E32A92 CRC64;
     MACRWSTKES PRWRSALLLL FLAGVYGNGA LAEHSENVHI SGVSTACGET PEQIRAPSGI
     ITSPGWPSEY PAKINCSWFI RANPGEIITI SFQDFDIQGS RRCNLDWLTI ETYKNIESYR
     ACGSTIPPPY ISSQDHIWIR FHSDDNISRK GFRLAYFSGK SEEPNCACDQ FRCGNGKCIP
     EAWKCNNMDE CGDSSDEEIC AKEANPPTAA AFQPCAYNQF QCLSRFTKVY TCLPESLKCD
     GNIDCLDLGD EIDCDVPTCG QWLKYFYGTF NSPNYPDFYP PGSNCTWLID TGDHRKVILR
     FTDFKLDGTG YGDYVKIYDG LEENPHKLLR VLTAFDSHAP LTVVSSSGQI RVHFCADKVN
     AARGFNATYQ VDGFCLPWEI PCGGNWGCYT EQQRCDGYWH CPNGRDETNC TMCQKEEFPC
     SRNGVCYPRS DRCNYQNHCP NGSDEKNCFF CQPGNFHCKN NRCVFESWVC DSQDDCGDGS
     DEENCPVIVP TRVITAAVIG SLICGLLLVI ALGCTCKLYS LRMFERRSFE TQLSRVEAEL
     LRREAPPSYG QLIAQGLIPP VEDFPVCSPN QASVLENLRL AVRSQLGFTS VRLPMAGRSS
     NIWNRIFNFA RSRHSGSLAL VSADGDEVVP SQSTSREPER NHTHRSLFSV ESDDTDTENE
     RRDMAGASGG VAAPLPQKVP PTTAVEATVG ACASSSTQST RGGHADNGRD VTSVEPPSVS
     PARHQLTSAL SRMTQGLRWV RFTLGRSSSL SQNQSPLRQL DNGVSGREDD DDVEMLIPIS
     DGSSDFDVND CSRPLLDLAS DQGQGLRQPY NATNPGVRPS NRDGPCERCG IVHTAQIPDT
     CLEVTLKNET SDDEALLLC
 
 
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