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FILA2_MOUSE
ID   FILA2_MOUSE             Reviewed;        2362 AA.
AC   Q2VIS4; Q8CB36;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Filaggrin-2;
DE            Short=FLG-2;
DE   AltName: Full=Intermediate filament-associated protein;
GN   Name=Flg2;
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].
RC   STRAIN=129/SvJ;
RA   Listwan P., Rothnagel J.A.;
RT   "FLG-2, a novel repetitive protein that is abundantly expressed in
RT   mammalian epidermis and functionally related to filaggrin.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2047-2362.
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198; SER-1204; SER-1205;
RP   SER-1278; SER-1284; SER-1285; SER-1356; SER-1362; SER-1363; SER-1438;
RP   SER-1439; SER-1510; SER-1516; SER-1517; SER-1590; SER-1596; SER-1597;
RP   SER-1744; SER-1750; SER-1751; SER-1824; SER-1830; SER-1831; SER-1902;
RP   SER-1908; SER-1909; SER-1980; SER-1986; SER-1987 AND SER-2104, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Essential for normal cell-cell adhesion in the cornified cell
CC       layers. Important for proper integrity and mechanical strength of the
CC       stratum corneum of the epidermis. {ECO:0000250|UniProtKB:Q5D862}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5D862}.
CC       Cytoplasmic granule {ECO:0000250|UniProtKB:Q5D862}.
CC   -!- PTM: Deiminated by PADI1, PADI2 or PADI3 in vitro. The deiminated form
CC       is degraded by calpain-1/CAPN1 more quickly and into shorter peptides
CC       than the intact protein. {ECO:0000250|UniProtKB:Q5D862}.
CC   -!- PTM: May be processed by calpain-1/CAPN1.
CC       {ECO:0000250|UniProtKB:Q5D862}.
CC   -!- SIMILARITY: Belongs to the S100-fused protein family. {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the S-100 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29615.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DQ118292; AAZ99028.1; -; Genomic_DNA.
DR   EMBL; AK036878; BAC29615.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001013826.1; NM_001013804.1.
DR   AlphaFoldDB; Q2VIS4; -.
DR   SMR; Q2VIS4; -.
DR   BioGRID; 230864; 1.
DR   STRING; 10090.ENSMUSP00000096482; -.
DR   iPTMnet; Q2VIS4; -.
DR   PhosphoSitePlus; Q2VIS4; -.
DR   jPOST; Q2VIS4; -.
DR   PaxDb; Q2VIS4; -.
DR   PRIDE; Q2VIS4; -.
DR   ProteomicsDB; 266849; -.
DR   GeneID; 229574; -.
DR   KEGG; mmu:229574; -.
DR   UCSC; uc029unl.1; mouse.
DR   CTD; 388698; -.
DR   MGI; MGI:3645678; Flg2.
DR   eggNOG; ENOG502QQH0; Eukaryota.
DR   InParanoid; Q2VIS4; -.
DR   OrthoDB; 1315634at2759; -.
DR   PhylomeDB; Q2VIS4; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 229574; 2 hits in 51 CRISPR screens.
DR   PRO; PR:Q2VIS4; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q2VIS4; protein.
DR   GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0036457; C:keratohyalin granule; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0048730; P:epidermis morphogenesis; ISS:UniProtKB.
DR   GO; GO:0061436; P:establishment of skin barrier; IBA:GO_Central.
DR   CDD; cd00213; S-100; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR034325; S-100_dom.
DR   InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00303; S100_CABP; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..2362
FT                   /note="Filaggrin-2"
FT                   /id="PRO_0000331455"
FT   DOMAIN          8..43
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          49..84
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REPEAT          261..308
FT                   /note="Filaggrin 1"
FT   REPEAT          373..414
FT                   /note="Filaggrin 2"
FT   REPEAT          555..607
FT                   /note="Filaggrin 3"
FT   REPEAT          672..723
FT                   /note="Filaggrin 4"
FT   REPEAT          880..927
FT                   /note="Filaggrin 5"
FT   REPEAT          984..1035
FT                   /note="Filaggrin 6"
FT   REPEAT          1165..1210
FT                   /note="Filaggrin 7"
FT   REPEAT          1280..1334
FT                   /note="Filaggrin 8"
FT   REPEAT          1474..1522
FT                   /note="Filaggrin 9"
FT   REPEAT          1723..1756
FT                   /note="Filaggrin 10"
FT   REPEAT          2016..2070
FT                   /note="Filaggrin 11"
FT   REPEAT          2218..2259
FT                   /note="Filaggrin 12"
FT   REGION          1..81
FT                   /note="S-100-like"
FT                   /evidence="ECO:0000250"
FT   REGION          96..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..2109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..777
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..929
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..954
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        971..985
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1039
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1063
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1199..1215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1221..1275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1279..1295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1301..1317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1327..1353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1357..1396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1400..1435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1455..1471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1478..1507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1511..1527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1558..1587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1613..1627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1634..1663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1667..1683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1712..1740
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1745..1769
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1770..1785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1792..1821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1828..1843
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1847..1863
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1870..1899
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1903..1919
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1925..1977
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1981..1997
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2003..2082
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         1198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1363
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1516
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1590
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1596
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1597
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1744
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1750
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1751
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1824
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1830
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1831
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1902
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1908
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1909
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1980
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1986
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1987
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        2118
FT                   /note="N -> H (in Ref. 1; AAZ99028)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2362 AA;  251372 MW;  F3FB473737052808 CRC64;
     MAYLLRSVVT IIDVFYKYTK QDEECGTLSK DELKELLEKE FRPILKNPDD PDTVDVIMHM
     LDRDHDRRLD FTEFILMIFK LALACNKVLG KEYCKASGSK KHRRGHQHQE EESETEEEEE
     TPRQKSGFRF SSWSEGEEHG HSSGGSRGPA KHRRGSNSKR LERQDELSSS EESRKKHHGS
     IFGHSWSSNK EKDGSRSEEL GEKGDKSYDS PSRESEEEYE SGYRLNHQGR EGHSGLSCGL
     EKNKYELNYI QLRKGGEQKL GYNTSSSGNS KIQSHVYGFS NSSGCCRPKN ASSSCQASRS
     QGQGNQSCRT QSNCQSGTSG GQGYGCVSEG QSSRCCQPKP RSCSQSSSQR GYGSKQCGQP
     QNCGRQQRMG SSHSSCCGPY GSGATQSSGC GQQRMSSCGH SSSSHQKGCS SNGFSKGDQR
     ASGSGHSSCC EQHGTNSSQS SGFKQHGHES GQSCCGQHGT ASSQSSGYSQ HRVGSGQSCH
     YGQHGSSSGQ SSSSGRHGSG SGQSSSSRHN RSGSSQSSGL EEHGSSSHQS HSSGHHGSGS
     RQSSGSEQHG AVSGQSSGSG KHETGPSQSS SSGHHGSGSQ QHGGGSGQST GFGEHESSSG
     HSSSSGQHRS GSRHSSGSGK HESGRSQSSG SGHHGSGSQQ HGGGSGNSTG FGEHGSSSHP
     LPSSGQNESS SGQSSRSERH GTGSGQSSGF GQHGSGSHQS SSSGHNEYGS GQTSSSWPHG
     KGSGQESGYG EQESGHGQSS SSWQHGTGPG QSSSSEEEES RPGQSSSSWQ HGKGSGQESG
     YGEQEAGHGQ SSSSWQHGTG AGNQSSGYGE HKSGPSHSSR SWHHGTGSGQ SLGFGQHGKG
     SHQSESSGHY ESVSEPSSSS WQHGNGSGES YGYGEHESGH GQSSSAWNHG NESGQSNGYG
     EHESGHGQSS SAWNHGNESG QSNGFGENES GRDQEGYQQR ESFHGQHRHP LSQHEQHSQF
     GYGRSPRSPV HPESSEGEEH SVVPRRYSGY GHGQGQAGHQ QRESGYGQRG RPQGPSQDSS
     RQPQAGHGQP SQSGYGRSPR RSQVHPEYSE GEAHSEVSQR HSGSSHCHCH CHGQARHQQR
     ESVHGQRGRP QGPSQDSSRH PQAGPGQPSQ SGSRRSPRSQ PVHPESSEGE EHSVVPQRHS
     GSGHGHGQGQ GQAGHQQRES VHGQQGRPQG PSQDSSRQPQ AGQGQPSQSG SGRSPRRSPV
     HPESSEGEEH SVVPQRHSGS GHGHGQGQGQ GQAGHQQRES VHGQRSRPQG PFQDSSRQPQ
     AGQGQPSQSG SGRSPRRSPV HPESSEGEEH SVVPQRHSGS GHGHGQGQGQ AGHQQRESVH
     GQPVRPEVPT QDSSRQPQAG QGQPSQSGSG RSPRRSPVHP ESSEGEEHSV VPQRNSESCH
     CHCHDQAGHQ QRESVHGQRG RPQGPSQDSS RHPQAGPGQP SQSGSRRSPR SSPVHPESSE
     GEEHSVVPQR HSGSGHGHGQ GQGQAGHQQR ESVHGQRGRP QGPTQDSSRQ PQAGQGQPSQ
     SGSGRSPRRS PVHPESSEGE EHSVVPQRHS GSGHGHGHGQ GQGQAGHQQR ESVHGQRGRP
     QGPSQDSSRQ PQAGQGQPSQ SGSGRSPRRS PVHPESSEGE EHSVVPQRYS GSGHGHGQGQ
     AGHQQRESVH GQRGRPQGPS QDSSRQPQAG QGQPSQSGSG RSPRRSPVHP ESSEGEEHSV
     IPQRHSGSGH SHGQGQVHAE HQQRESVHGQ RGRPQGPSQD SSRQPQAGQG QPSLSGSGRS
     PRRSPVHPES SEGEEHSVVP QRHSHSESGH GHGQGQGQAG HQQRESVHGQ RGRPQGPSQD
     SSRQPQAGQG QPSQSGSGRS PGRSPVHPES SEGEEHSVVP QRHSESGHGH GQGQGQAGHQ
     QRESVHGQRG RPQGPSQDSS RQPQAGQGQP SQSGSGRSPR RSPVHPESSE GEEHSVVPQR
     HSGSGHGHGQ GQGQAGHQQR ESVHGQPVRP QGPSQDSSSQ PQASQGQPSQ SGSGRSPRRS
     PVHPESSEGE EHSVVPQRHS GSGHGHGQGQ GQAGHQQRES LHGQRGRSQS PFHPSHSIHW
     QSKCTISKKS SRLSGHYGRN HFQSTISGNQ YDSSQSSRHG SYGPQDYDYG QSGYGPSGRL
     RSNSQSSIPF SSAHRATNME VLPCGQSFSP SDHVGTKANE QIGELVFKYR ESETGPDQSV
     DYYNLTESNS TTRGHECSHG HSVVVPEHSD DSDFNYGHSY NGKQQICQSQ PTVQSCFDDS
     QYILFQKHLE SPSFGNQSGF SPNERQLYTC NESIDSYHLS SDSNNRNQIY SSNNSFPNLY
     CIGTEQCIYL PSATILGEGT EGQEPGYTQP GTICKYNQFL DGRKSRTRGN HETGKMKSGS
     AYLDSNTPLY TYVQEQKSYY FE
 
 
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