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FETA_HUMAN
ID   FETA_HUMAN              Reviewed;         609 AA.
AC   P02771; B2RBU3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 211.
DE   RecName: Full=Alpha-fetoprotein;
DE   AltName: Full=Alpha-1-fetoprotein;
DE   AltName: Full=Alpha-fetoglobulin;
DE   Flags: Precursor;
GN   Name=AFP; Synonyms=HPAFP;
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].
RX   PubMed=6192439; DOI=10.1073/pnas.80.15.4604;
RA   Morinaga T., Sakai M., Wegmann T.G., Tamaoki T.;
RT   "Primary structures of human alpha-fetoprotein and its mRNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:4604-4608(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2436661; DOI=10.1021/bi00379a020;
RA   Gibbs P.E.M., Zielinski R., Boyd C., Dugaiczyk A.;
RT   "Structure, polymorphism, and novel repeated DNA elements revealed by a
RT   complete sequence of the human alpha-fetoprotein gene.";
RL   Biochemistry 26:1332-1343(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-570.
RC   TISSUE=Heart;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 AND 596-609, AND GENE STRUCTURE.
RX   PubMed=2580830; DOI=10.1016/s0021-9258(18)89178-5;
RA   Sakai M., Morinaga T., Urano Y., Watanabe K., Wegmann T.G., Tamaoki T.;
RT   "The human alpha-fetoprotein gene. Sequence organization and the 5'
RT   flanking region.";
RL   J. Biol. Chem. 260:5055-5060(1985).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, AND INVOLVEMENT IN HPAFP.
RX   PubMed=7684942; DOI=10.1093/hmg/2.4.379;
RA   McVey J.H., Michaelides K., Hansen L.P., Ferguson-Smith M., Tilghman S.,
RA   Krumlauf R., Tuddenham E.G.D.;
RT   "A G-->A substitution in an HNF I binding site in the human alpha-
RT   fetoprotein gene is associated with hereditary persistence of alpha-
RT   fetoprotein (HPAFP).";
RL   Hum. Mol. Genet. 2:379-384(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 311-332; 348-372 AND 422-437, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Vishwanath V.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 429-556.
RX   PubMed=6187626; DOI=10.1016/0378-1119(82)90210-4;
RA   Beattie W.G., Dugaiczyk A.;
RT   "Structure and evolution of human alpha-fetoprotein deduced from partial
RT   sequence of cloned cDNA.";
RL   Gene 20:415-422(1982).
RN   [9]
RP   PROTEIN SEQUENCE OF 19-609.
RX   PubMed=1709810; DOI=10.1021/bi00234a032;
RA   Pucci P., Siciliano R., Malorni A., Marino G., Tecce M.F., Ceccarini C.,
RA   Terrana B.;
RT   "Human alpha-fetoprotein primary structure: a mass spectrometric study.";
RL   Biochemistry 30:5061-5066(1991).
RN   [10]
RP   PRELIMINARY PROTEIN SEQUENCE OF 19-35.
RX   PubMed=70228; DOI=10.1016/0005-2795(77)90198-2;
RA   Yachnin S., Hsu R., Heinrikson R.L., Miller J.B.;
RT   "Studies on human alpha-fetoprotein. Isolation and characterization of
RT   monomeric and polymeric forms and amino-terminal sequence analysis.";
RL   Biochim. Biophys. Acta 493:418-428(1977).
RN   [11]
RP   PRELIMINARY PROTEIN SEQUENCE OF 19-38.
RX   PubMed=71198;
RA   Aoyagi Y., Ikenaka T., Ichida F.;
RT   "Comparative chemical structures of human alpha-fetoproteins from fetal
RT   serum and from ascites fluid of a patient with hepatoma.";
RL   Cancer Res. 37:3663-3667(1977).
RN   [12]
RP   PRELIMINARY PROTEIN SEQUENCE OF 19-39.
RX   PubMed=4138095;
RA   Ruoslahti E., Pihko H., Vaheri A., Seppala M., Virolainen M., Konttinen A.;
RT   "Alpha fetoprotein: structure and expression in man and inbred mouse
RT   strains under normal conditions and liver injury.";
RL   Johns Hopkins Med. J. Suppl. 3:249-255(1974).
RN   [13]
RP   METAL-BINDING.
RX   PubMed=80265;
RA   Aoyagi Y., Ikenaka T., Ichida F.;
RT   "Copper(II)-binding ability of human alpha-fetoprotein.";
RL   Cancer Res. 38:3483-3486(1978).
RN   [14]
RP   BILIRUBIN-BINDING.
RX   PubMed=89900;
RA   Aoyagi Y., Ikenaka T., Ichida F.;
RT   "Alpha-fetoprotein as a carrier protein in plasma and its bilirubin-binding
RT   ability.";
RL   Cancer Res. 39:3571-3574(1979).
RN   [15]
RP   SULFATION.
RX   PubMed=2414772; DOI=10.1073/pnas.82.21.7160;
RA   Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.;
RT   "Tyrosine sulfation of proteins from the human hepatoma cell line HepG2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985).
RN   [16]
RP   INVOLVEMENT IN AFPD.
RX   PubMed=15280901; DOI=10.1038/sj.ejhg.5201246;
RA   Sharony R., Zadik I., Parvari R.;
RT   "Congenital deficiency of alpha feto-protein.";
RL   Eur. J. Hum. Genet. 12:871-874(2004).
RN   [17]
RP   INVOLVEMENT IN AFPD.
RX   PubMed=18854864; DOI=10.1038/ejhg.2008.186;
RA   Petit F.M., Hebert M., Picone O., Brisset S., Maurin M.L., Parisot F.,
RA   Capel L., Benattar C., Senat M.V., Tachdjian G., Labrune P.;
RT   "A new mutation in the AFP gene responsible for a total absence of alpha
RT   feto-protein on second trimester maternal serum screening for Down
RT   syndrome.";
RL   Eur. J. Hum. Genet. 17:387-390(2009).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   PHOSPHORYLATION AT SER-111; SER-115; SER-117; SER-344; SER-444 AND SER-445.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
CC   -!- FUNCTION: Binds copper, nickel, and fatty acids as well as, and
CC       bilirubin less well than, serum albumin. Only a small percentage (less
CC       than 2%) of the human AFP shows estrogen-binding properties.
CC   -!- SUBUNIT: Dimeric and trimeric forms have been found in addition to the
CC       monomeric form.
CC   -!- INTERACTION:
CC       P02771; PRO_0000045596 [Q99IB8]; Xeno; NbExp=2; IntAct=EBI-722498, EBI-6901449;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma. Synthesized by the fetal liver and yolk
CC       sac.
CC   -!- DEVELOPMENTAL STAGE: Occurs in the plasma of fetuses more than 4 weeks
CC       old, reaches the highest levels during the 12th-16th week of gestation,
CC       and drops to trace amounts after birth. The serum level in adults is
CC       usually less than 40 ng/ml. AFP occurs also at high levels in the
CC       plasma and ascitic fluid of adults with hepatoma.
CC   -!- PTM: Independent studies suggest heterogeneity of the N-terminal
CC       sequence of the mature protein and of the cleavage site of the signal
CC       sequence.
CC   -!- PTM: Sulfated. {ECO:0000269|PubMed:2414772}.
CC   -!- DISEASE: Alpha-fetoprotein deficiency (AFPD) [MIM:615969]: A benign
CC       condition characterized by undetectable AFP levels in the amniotic
CC       fluid. Affected individuals are asymptomatic and present normal
CC       development. {ECO:0000269|PubMed:15280901,
CC       ECO:0000269|PubMed:18854864}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Alpha-fetoprotein, hereditary persistence (HPAFP)
CC       [MIM:615970]: A benign autosomal dominant condition characterized by
CC       continued expression of alpha-fetoprotein in adult life.
CC       {ECO:0000269|PubMed:7684942}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00769}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-fetoprotein entry;
CC       URL="https://en.wikipedia.org/wiki/Alpha-fetoprotein";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/AFPID44248ch4q13.html";
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DR   EMBL; V01514; CAA24758.1; -; mRNA.
DR   EMBL; M16110; AAB58754.1; -; Genomic_DNA.
DR   EMBL; AK314817; BAG37340.1; -; mRNA.
DR   EMBL; BC027881; AAH27881.1; -; mRNA.
DR   EMBL; M10949; AAA51674.1; -; Genomic_DNA.
DR   EMBL; M10950; AAA51675.1; -; Genomic_DNA.
DR   EMBL; Z19532; CAA79592.1; -; Genomic_DNA.
DR   CCDS; CCDS3556.1; -.
DR   PIR; A26624; FPHU.
DR   RefSeq; NP_001125.1; NM_001134.2.
DR   PDB; 3MRK; X-ray; 1.40 A; P=137-145.
DR   PDBsum; 3MRK; -.
DR   AlphaFoldDB; P02771; -.
DR   SMR; P02771; -.
DR   BioGRID; 106682; 19.
DR   IntAct; P02771; 10.
DR   STRING; 9606.ENSP00000379138; -.
DR   ChEMBL; CHEMBL3712864; -.
DR   GlyConnect; 41; 31 N-Linked glycans (2 sites).
DR   GlyGen; P02771; 3 sites, 48 N-linked glycans (3 sites).
DR   iPTMnet; P02771; -.
DR   PhosphoSitePlus; P02771; -.
DR   BioMuta; AFP; -.
DR   DMDM; 120042; -.
DR   jPOST; P02771; -.
DR   MassIVE; P02771; -.
DR   MaxQB; P02771; -.
DR   PaxDb; P02771; -.
DR   PeptideAtlas; P02771; -.
DR   PRIDE; P02771; -.
DR   ProteomicsDB; 51589; -.
DR   TopDownProteomics; P02771; -.
DR   ABCD; P02771; 16 sequenced antibodies.
DR   Antibodypedia; 1359; 3533 antibodies from 57 providers.
DR   DNASU; 174; -.
DR   Ensembl; ENST00000395792.7; ENSP00000379138.2; ENSG00000081051.8.
DR   GeneID; 174; -.
DR   KEGG; hsa:174; -.
DR   MANE-Select; ENST00000395792.7; ENSP00000379138.2; NM_001134.3; NP_001125.1.
DR   UCSC; uc003hgz.3; human.
DR   CTD; 174; -.
DR   DisGeNET; 174; -.
DR   GeneCards; AFP; -.
DR   HGNC; HGNC:317; AFP.
DR   HPA; ENSG00000081051; Tissue enriched (liver).
DR   MalaCards; AFP; -.
DR   MIM; 104150; gene.
DR   MIM; 615969; phenotype.
DR   MIM; 615970; phenotype.
DR   neXtProt; NX_P02771; -.
DR   OpenTargets; ENSG00000081051; -.
DR   Orphanet; 168612; Congenital deficiency in alpha-fetoprotein.
DR   Orphanet; 168615; Hereditary persistence of alpha-fetoprotein.
DR   PharmGKB; PA24614; -.
DR   VEuPathDB; HostDB:ENSG00000081051; -.
DR   eggNOG; ENOG502R7EA; Eukaryota.
DR   GeneTree; ENSGT00390000000113; -.
DR   HOGENOM; CLU_030161_1_0_1; -.
DR   InParanoid; P02771; -.
DR   OMA; HEECCRG; -.
DR   OrthoDB; 906547at2759; -.
DR   PhylomeDB; P02771; -.
DR   TreeFam; TF335561; -.
DR   PathwayCommons; P02771; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SignaLink; P02771; -.
DR   SIGNOR; P02771; -.
DR   BioGRID-ORCS; 174; 14 hits in 1075 CRISPR screens.
DR   ChiTaRS; AFP; human.
DR   GeneWiki; Alpha-fetoprotein; -.
DR   GenomeRNAi; 174; -.
DR   Pharos; P02771; Tbio.
DR   PRO; PR:P02771; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P02771; protein.
DR   Bgee; ENSG00000081051; Expressed in right lobe of liver and 110 other tissues.
DR   ExpressionAtlas; P02771; baseline and differential.
DR   Genevisible; P02771; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
DR   GO; GO:0042448; P:progesterone metabolic process; IEA:Ensembl.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR   CDD; cd00015; ALBUMIN; 3.
DR   InterPro; IPR000264; ALB/AFP/VDB.
DR   InterPro; IPR020858; Serum_albumin-like.
DR   InterPro; IPR021177; Serum_albumin/AFP/Afamin.
DR   InterPro; IPR020857; Serum_albumin_CS.
DR   InterPro; IPR014760; Serum_albumin_N.
DR   PANTHER; PTHR11385; PTHR11385; 1.
DR   Pfam; PF00273; Serum_albumin; 3.
DR   PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
DR   PRINTS; PR00803; AFETOPROTEIN.
DR   PRINTS; PR00802; SERUMALBUMIN.
DR   SMART; SM00103; ALBUMIN; 3.
DR   SUPFAM; SSF48552; SSF48552; 3.
DR   PROSITE; PS00212; ALBUMIN_1; 2.
DR   PROSITE; PS51438; ALBUMIN_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Metal-binding; Nickel; Phosphoprotein; Reference proteome;
KW   Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:1709810"
FT   CHAIN           19..609
FT                   /note="Alpha-fetoprotein"
FT                   /id="PRO_0000001097"
FT   DOMAIN          19..210
FT                   /note="Albumin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          211..402
FT                   /note="Albumin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          403..601
FT                   /note="Albumin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   BINDING         22
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000269|PubMed:80265"
FT   MOD_RES         111
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         115
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         117
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         344
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         444
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         445
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /id="CAR_000070"
FT   DISULFID        99..114
FT   DISULFID        113..124
FT   DISULFID        148..193
FT   DISULFID        192..201
FT   DISULFID        224..270
FT   DISULFID        269..277
FT   DISULFID        289..303
FT   DISULFID        302..313
FT   DISULFID        384..393
FT   DISULFID        416..462
FT   DISULFID        461..472
FT   DISULFID        485..501
FT   DISULFID        500..511
FT   DISULFID        538..583
FT   DISULFID        582..591
FT   VARIANT         187
FT                   /note="K -> Q (in dbSNP:rs35765619)"
FT                   /id="VAR_033928"
FT   VARIANT         570
FT                   /note="A -> G (in dbSNP:rs7790)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_012049"
SQ   SEQUENCE   609 AA;  68678 MW;  4D4E45820E1C2D4F CRC64;
     MKWVESIFLI FLLNFTESRT LHRNEYGIAS ILDSYQCTAE ISLADLATIF FAQFVQEATY
     KEVSKMVKDA LTAIEKPTGD EQSSGCLENQ LPAFLEELCH EKEILEKYGH SDCCSQSEEG
     RHNCFLAHKK PTPASIPLFQ VPEPVTSCEA YEEDRETFMN KFIYEIARRH PFLYAPTILL
     WAARYDKIIP SCCKAENAVE CFQTKAATVT KELRESSLLN QHACAVMKNF GTRTFQAITV
     TKLSQKFTKV NFTEIQKLVL DVAHVHEHCC RGDVLDCLQD GEKIMSYICS QQDTLSNKIT
     ECCKLTTLER GQCIIHAEND EKPEGLSPNL NRFLGDRDFN QFSSGEKNIF LASFVHEYSR
     RHPQLAVSVI LRVAKGYQEL LEKCFQTENP LECQDKGEEE LQKYIQESQA LAKRSCGLFQ
     KLGEYYLQNA FLVAYTKKAP QLTSSELMAI TRKMAATAAT CCQLSEDKLL ACGEGAADII
     IGHLCIRHEM TPVNPGVGQC CTSSYANRRP CFSSLVVDET YVPPAFSDDK FIFHKDLCQA
     QGVALQTMKQ EFLINLVKQK PQITEEQLEA VIADFSGLLE KCCQGQEQEV CFAEEGQKLI
     SKTRAALGV
 
 
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