位置:首页 > 蛋白库 > CELR3_RAT
CELR3_RAT
ID   CELR3_RAT               Reviewed;        3313 AA.
AC   O88278;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 3;
DE   AltName: Full=Multiple epidermal growth factor-like domains protein 2;
DE            Short=Multiple EGF-like domains protein 2;
DE   Flags: Precursor;
GN   Name=Celsr3; Synonyms=Megf2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA   Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT   "Identification of high-molecular-weight proteins with multiple EGF-like
RT   motifs by motif-trap screening.";
RL   Genomics 51:27-34(1998).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2117; TYR-3050 AND SER-3098,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC   -!- FUNCTION: Receptor that may have an important role in cell/cell
CC       signaling during nervous system formation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain. Expressed in cerebellum,
CC       olfactory bulb, cerebral cortex, hippocampus and brain stem.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC       and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB011528; BAA32459.1; -; mRNA.
DR   RefSeq; NP_112610.1; NM_031320.1.
DR   SMR; O88278; -.
DR   STRING; 10116.ENSRNOP00000041011; -.
DR   GlyGen; O88278; 15 sites.
DR   iPTMnet; O88278; -.
DR   PhosphoSitePlus; O88278; -.
DR   PaxDb; O88278; -.
DR   PRIDE; O88278; -.
DR   Ensembl; ENSRNOT00000112823; ENSRNOP00000079747; ENSRNOG00000053889.
DR   GeneID; 83466; -.
DR   KEGG; rno:83466; -.
DR   UCSC; RGD:621787; rat.
DR   CTD; 1951; -.
DR   RGD; 621787; Celsr3.
DR   eggNOG; KOG4289; Eukaryota.
DR   GeneTree; ENSGT00940000160077; -.
DR   HOGENOM; CLU_000158_1_0_1; -.
DR   InParanoid; O88278; -.
DR   OMA; WGSPSCG; -.
DR   OrthoDB; 23882at2759; -.
DR   PhylomeDB; O88278; -.
DR   PRO; PR:O88278; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000053889; Expressed in cerebellum and 7 other tissues.
DR   Genevisible; O88278; RN.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007413; P:axonal fasciculation; ISO:RGD.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR   GO; GO:0036514; P:dopaminergic neuron axon guidance; ISO:RGD.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0001764; P:neuron migration; ISO:RGD.
DR   GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; ISO:RGD.
DR   GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0036515; P:serotonergic neuron axon guidance; ISO:RGD.
DR   CDD; cd00055; EGF_Lam; 2.
DR   CDD; cd00110; LamG; 2.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 4.10.1240.10; -; 1.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR002049; LE_dom.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF00028; Cadherin; 8.
DR   Pfam; PF00008; EGF; 3.
DR   Pfam; PF16489; GAIN; 1.
DR   Pfam; PF02793; HRM; 1.
DR   Pfam; PF00053; Laminin_EGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00112; CA; 9.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM00180; EGF_Lam; 1.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF111418; SSF111418; 1.
DR   SUPFAM; SSF49313; SSF49313; 9.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00232; CADHERIN_1; 7.
DR   PROSITE; PS50268; CADHERIN_2; 8.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Developmental protein; Disulfide bond;
KW   EGF-like domain; G-protein coupled receptor; Glycoprotein; Hydroxylation;
KW   Laminin EGF-like domain; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..3313
FT                   /note="Cadherin EGF LAG seven-pass G-type receptor 3"
FT                   /id="PRO_0000012920"
FT   TOPO_DOM        32..2538
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2539..2559
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2560..2570
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2571..2591
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2592..2599
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2600..2620
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2621..2641
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2642..2662
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2663..2679
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2680..2700
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2701..2724
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2725..2745
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2746..2752
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2753..2773
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2774..3313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          317..424
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          425..536
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          537..642
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          643..747
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          748..849
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          850..952
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          953..1058
FT                   /note="Cadherin 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1059..1160
FT                   /note="Cadherin 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1161..1257
FT                   /note="Cadherin 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1366..1424
FT                   /note="EGF-like 1; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1426..1462
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1466..1505
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1506..1710
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1713..1749
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1753..1935
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1937..1972
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1973..2011
FT                   /note="EGF-like 6; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          2012..2044
FT                   /note="EGF-like 7; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          2046..2081
FT                   /note="EGF-like 8; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          2068..2115
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          2475..2527
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          148..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2356..2395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2887..2927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2977..3004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3091..3242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3255..3313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2360..2386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2978..2999
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3109..3124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3197..3211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3255..3303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1954
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2117
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:16641100"
FT   MOD_RES         3050
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:16641100"
FT   MOD_RES         3098
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16641100"
FT   CARBOHYD        623
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        838
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1640
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1704
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1761
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2044
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2472
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2504
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1370..1381
FT                   /evidence="ECO:0000250"
FT   DISULFID        1375..1412
FT                   /evidence="ECO:0000250"
FT   DISULFID        1414..1423
FT                   /evidence="ECO:0000250"
FT   DISULFID        1430..1441
FT                   /evidence="ECO:0000250"
FT   DISULFID        1435..1450
FT                   /evidence="ECO:0000250"
FT   DISULFID        1452..1461
FT                   /evidence="ECO:0000250"
FT   DISULFID        1470..1481
FT                   /evidence="ECO:0000250"
FT   DISULFID        1475..1491
FT                   /evidence="ECO:0000250"
FT   DISULFID        1493..1504
FT                   /evidence="ECO:0000250"
FT   DISULFID        1684..1710
FT                   /evidence="ECO:0000250"
FT   DISULFID        1717..1728
FT                   /evidence="ECO:0000250"
FT   DISULFID        1722..1737
FT                   /evidence="ECO:0000250"
FT   DISULFID        1739..1748
FT                   /evidence="ECO:0000250"
FT   DISULFID        1906..1935
FT                   /evidence="ECO:0000250"
FT   DISULFID        1941..1952
FT                   /evidence="ECO:0000250"
FT   DISULFID        1946..1961
FT                   /evidence="ECO:0000250"
FT   DISULFID        1963..1972
FT                   /evidence="ECO:0000250"
FT   DISULFID        1976..1987
FT                   /evidence="ECO:0000250"
FT   DISULFID        1981..1999
FT                   /evidence="ECO:0000250"
FT   DISULFID        2001..2010
FT                   /evidence="ECO:0000250"
FT   DISULFID        2018..2031
FT                   /evidence="ECO:0000250"
FT   DISULFID        2033..2043
FT                   /evidence="ECO:0000250"
FT   DISULFID        2050..2065
FT                   /evidence="ECO:0000250"
FT   DISULFID        2052..2068
FT                   /evidence="ECO:0000250"
FT   DISULFID        2070..2080
FT                   /evidence="ECO:0000250"
FT   DISULFID        2089..2098
FT                   /evidence="ECO:0000250"
FT   DISULFID        2101..2113
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   3313 AA;  359355 MW;  B11DA09517288764 CRC64;
     MARRPLWWGL PGPSTPLLLL LLFSLFPSSR EEMGGGGDQG WDPGVATATG PRAQIGSGAV
     ALCPESPGVW EDGDPGLGVR EPVFMKLRVG RQNARNGRGA PEQPNREPVV QALGSREQEA
     GQGSGYLLCW HPEISSCGRT GHLRRGSLPL DALSPGDSDL RNSSPHPSEL LAQPDSPRPV
     AFQRNGRRSI RKRVETFRCC GKLWEPGHKG QGERSATSTV DRGPLRRDCL PGSLGSGLGE
     DSAPRAVRTA PAPGSAPHES RTAPERMRSR GLFRRGFLFE RPGPRPPGFP TGAEAKRILS
     TNQARSRRAA NRHPQFPQYN YQTLVPENEA AGTAVLRVVA QDPDPGEAGR LVYSLAALMN
     SRSLELFSID PQSGLIRTAA ALDRESMERH YLRVTAQDHG SPRLSATTMV AVTVADRNDH
     APVFEQAQYR ETLRENVEEG YPILQLRATD GDAPPNANLR YRFVGSPAAR TAAAAAFEID
     PRSGLISTSG RVDREHMESY ELVVEASDQG QEPGPRSATV RVHITVLDEN DNAPQFSEKR
     YVAQVREDVR PHTVVLRVTA TDKDKDANGL VHYNIISGNS RGHFAIDSLT GEIQVMAPLD
     FEAEREYALR IRAQDAGRPP LSNNTGLASI QVVDINDHSP IFVSTPFQVS VLENAPLGHS
     VIHIQAVDAD HGENSRLEYS LTGVASDTPF VINSATGWVS VSGPLDRESV EHYFFGVEAR
     DHGSPPLSAS ASVTVTVLDV NDNRPEFTMK EYHLRLNEDA AVGTSVVSVT AVDRDANSAI
     SYQITGGNTR NRFAISTQGG MGLVTLALPL DYKQERYFKL VLTASDRALH DHCYVHINIT
     DANTHRPVFQ SAHYSVSMNE DRPVGSTVVV ISASDDDVGE NARITYLLED NLPQFRIDAD
     SGAITLQAPL DYEDQVTYTL AITARDNGIP QKADTTYVEV MVNDVNDNAP QFVASHYTGL
     VSEDAPPFTS VLQISATDRD AHANGRVQYT FQNGEDGDGD FTIEPTSGIV RTVRRLDREA
     VPVYELTAYA VDRGVPPLRT PVSIQVTVQD VNDNAPVFPA EEFEVRVKEN SIVGSVVAQI
     TAVDPDDGPN AHIMYQIVEG NIPELFQMDI FSGELTALID LDYEARQEYV IVVQATSAPL
     VSRATVHVRL VDQNDNSPVL NNFQILFNNY VSNRSDTFPS GIIGRIPAYD PDVSDHLFYS
     FERGNELQLL VVNQTSGELR LSRKLDNNRP LVASMLVTVT DGLHSVTAQC VLRVVIITEE
     LLANSLTVRL ENMWQERFLS PLLGHFLEGV AAVLATPTED VFIFNIQNDT DVGGTVLNVS
     FSALAPRGAG AGAAGPWFSS EELQEQLYVR RAALAARSLL DVLPFDDNVC LREPCENYMK
     CVSVLRFDSS APFLASASTL FRPIQPIAGL RCRCPPGFTG DFCETELDLC YSNPCRNGGA
     CARREGGYTC VCRPRFTGED CELDTEAGRC VPGVCRNGGT CTNAPNGGFR CQCPAGGAFE
     GPRCEVAARS FPPSSFVMFR GLRQRFHLTL SLSFATVQPS GLLFYNGRLN EKHDFLALEL
     VAGQVRLTYS TGESSTVVSP TVPGGLSDGQ WHTVHLRYYN KPRTDALGGA QGPSKDKVAV
     LSVDDCNVAV ALRFGAEIGN YSCAAAGVQT SSKKSLDLTG PLLLGGVPNL PENFPVSRKD
     FIGCMRDLHI DGRRVDMAAF VANNGTTAGC QAKSHFCASG PCKNGGLCSE RWGGFSCDCP
     VGFGGKDCRL TMAHPYHFQG NGTLSWDFGN DMPVSVPWYL GLSFRTRATK GVLMQVQLGP
     HSVLLCKLDQ GLLSVTLSRA SGHAVHLLLD QMTVSDGRWH DLRLELQEEP GGRRGHHIFM
     VSLDFTLFQD TMAMGSELEG LKVKHLHVGG PPPSSKEEGP QGLVGCIQGV WTGFTPFGSS
     ALPPPSHRIN VEPGCTVTNP CASGPCPPHA NCKDLWQTFS CTCWPGYYGP GCVDACLLNP
     CQNQGSCRHL QGGPHGYTCD CASGYFGQHC EHRMDQQCPR GWWGSPTCGP CNCDVHKGFD
     PNCNKTSGQC HCKEFHYRPR GSDSCLPCDC YPVGSTSRSC APHSGQCPCR PGALGRQCNS
     CDSPFAEVTA SGCRVLYDAC PKSLRSGVWW PQTKFGVLAT VPCPRGALGL RGTGAAVRLC
     DEDHGWLEPD FFNCTSPAFR ELSLLLDGLE LNKTALDTVE AKKLAQRLRE VTGQTDHYFS
     QDVRVTARLL AYLLAFESHQ QGFGLTATQD AHFNENLLWA GSALLAPETG DLWAALGQRA
     PGGSPGSAGL VRHLEEYAAT LARNMDLTYL NPVGLVTPNI MLSIDRMEQP SSSQGAHRYP
     RYHSNLFRGQ DAWDPHTHVL LPSQSPQPSP SEVLPTSSNA ENATASGVVS PPAPLEPESE
     PGISIVILLV YRALGGLLPA QFQAERRGAR LPQNPVMNSP VVSVAVFRGR NFLRGALVSP
     INLEFRLLQT ANRSKAICVQ WDPPGPADQH GMWTARDCEL VHRNGSHARC RCSRTGTFGV
     LMDASPRERL EGDLELLAVF THVVVAASVT ALVLTAAVLL SLRSLKSNVR GIHANVAAAL
     GVAELLFLLG IHRTHNQLLC TVVAILLHYF FLSTFAWLLV QGLHLYRMQV EPRNVDRGAM
     RFYHALGWGV PAVLLGLAVG LDPEGYGNPD FCWISIHEPL IWSFAGPIVL VIVMNGIMFL
     LAARTSCSTG QREAKKTSVL RTLRSSFLLL LLVSASWLFG LLAVNHSVLA FHYLHAGLCG
     LQGLAVLLLF CVLNADARAA WTPACLGKKA APEETRPAPG PGSGAYNNTA LFEESGLIRI
     TLGASTVSSV SSARSGRAQD QDSQRGRSYL RDNVLVRHGS TAEHAEHSLQ AHAGPTDLDV
     AMFHRDAGAD SDSDSDLSLE EERSLSIPSS ESEDNGRTRG RFQRPLRRAA QSERLLAHPK
     DVDGNDLLSY WPALGECEAA PCALQAWGSE RRLGLDSNKD AANNNQPELA LTSGDETSLG
     RAQRQRKGIL KNRLQYPLVP QTRGTPELSW CRAATLGHRA VPAASYGRIY AGGGTGSLSQ
     PASRYSSREQ LDLLLRRQLS RERLEEVPVP APVLHPLSRP GSQERLDTAP ARLEPRDRGS
     TLPRRQPPRD YPGTMAGRFG SRDALDLGAP REWLSTLPPP RRNRDLDPQH PPLPLSPQRP
     LSRDPLLPSR PLDSLSRISN SRERLDQVPS RHPSREALGP APQLLRARED PASGPSHGPS
     TEQLDILSSI LASFNSSALS SVQSSSTPSG PHTTATPSAT ASALGPSTPR SATSHSISEL
     SPDSEVPRSE GHS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024