位置:首页 > 蛋白库 > MUP4_CAEEL
MUP4_CAEEL
ID   MUP4_CAEEL              Reviewed;        2104 AA.
AC   Q21281; Q964N4;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 4.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Transmembrane matrix receptor MUP-4 {ECO:0000312|EMBL:AAK69172.1};
DE   AltName: Full=Muscle-positioning protein 4;
DE   Flags: Precursor;
GN   Name=mup-4 {ECO:0000312|EMBL:CCD63613.1, ECO:0000312|WormBase:K07D8.1};
GN   ORFNames=K07D8.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAK69172.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=11470827; DOI=10.1083/jcb.200007075;
RA   Hong L., Elbl T., Ward J., Franzini-Armstrong C., Rybicka K.K.,
RA   Gatewood B.K., Baillie D.L., Bucher E.A.;
RT   "MUP-4 is a novel transmembrane protein with functions in epithelial cell
RT   adhesion in Caenorhabditis elegans.";
RL   J. Cell Biol. 154:403-414(2001).
RN   [2] {ECO:0000312|EMBL:CCD63613.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD63613.1};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9136009; DOI=10.1093/genetics/146.1.165;
RA   Gatewood B.K., Bucher E.A.;
RT   "The mup-4 locus in Caenorhabditis elegans is essential for hypodermal
RT   integrity, organismal morphogenesis and embryonic body wall muscle
RT   position.";
RL   Genetics 146:165-183(1997).
CC   -!- FUNCTION: Required for junctional attachments between hypodermis and
CC       muscle, and between the apical epithelial surface and the cuticular
CC       matrix. Essential for enclosure of the embryo by the hypodermis,
CC       hypodermal integrity, embryo elongation, and maintenance of hypodermal
CC       morphology in fully elongated embryos. {ECO:0000269|PubMed:11470827,
CC       ECO:0000269|PubMed:9136009}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
CC       {ECO:0000269|PubMed:11470827}. Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:11470827}. Cell membrane {ECO:0000255}; Single-pass
CC       membrane protein {ECO:0000255}. Note=Detected in intermediate filaments
CC       and hemidesmosomes. {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Abundant at hypodermal cell-matrix junctions
CC       overlying muscle of threefold embryos. Expression continues in body
CC       wall muscle in larvae and adults and is also detected in other regions
CC       where cells show mechanical attachment to the hypodermis including the
CC       inner surface of the pharynx, overlying anal and intestinal muscles,
CC       overlying vulval and uterine sex muscles, male tail muscle attachment
CC       zones and the six mechanosensory neurons (at protein level).
CC       {ECO:0000269|PubMed:11470827}.
CC   -!- DEVELOPMENTAL STAGE: Expression detected in embryo, larva and adult.
CC       {ECO:0000269|PubMed:11470827}.
CC   -!- DISRUPTION PHENOTYPE: Arrested embryonic development either at bean or
CC       twofold stages with failure of hypodermis to enclose the embryo or at
CC       threefold stage with defects in hypodermal cell organization and muscle
CC       cell positioning. When disrupted in larvae, causes paralysis and
CC       displacement of muscles. {ECO:0000269|PubMed:11470827,
CC       ECO:0000269|PubMed:9136009}.
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; AF289202; AAK69172.1; -; mRNA.
DR   EMBL; FO080425; CCD63613.1; -; Genomic_DNA.
DR   RefSeq; NP_498645.1; NM_066244.6.
DR   AlphaFoldDB; Q21281; -.
DR   SMR; Q21281; -.
DR   BioGRID; 41268; 12.
DR   DIP; DIP-26346N; -.
DR   IntAct; Q21281; 2.
DR   STRING; 6239.K07D8.1; -.
DR   EPD; Q21281; -.
DR   PaxDb; Q21281; -.
DR   PeptideAtlas; Q21281; -.
DR   PRIDE; Q21281; -.
DR   EnsemblMetazoa; K07D8.1.1; K07D8.1.1; WBGene00003497.
DR   GeneID; 176060; -.
DR   KEGG; cel:CELE_K07D8.1; -.
DR   UCSC; K07D8.1.1; c. elegans.
DR   CTD; 176060; -.
DR   WormBase; K07D8.1; CE29511; WBGene00003497; mup-4.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00940000167387; -.
DR   HOGENOM; CLU_000420_0_0_1; -.
DR   InParanoid; Q21281; -.
DR   OMA; HGDCIHD; -.
DR   OrthoDB; 1174178at2759; -.
DR   PhylomeDB; Q21281; -.
DR   PRO; PR:Q21281; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003497; Expressed in larva and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030056; C:hemidesmosome; IDA:WormBase.
DR   GO; GO:0098733; C:hemidesmosome associated protein complex; IDA:WormBase.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR006150; Cys_repeat_1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000082; SEA_dom.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 7.
DR   Pfam; PF12661; hEGF; 3.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00181; EGF; 27.
DR   SMART; SM00179; EGF_CA; 19.
DR   SMART; SM00200; SEA; 2.
DR   SMART; SM00327; VWA; 1.
DR   SMART; SM00289; WR1; 3.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 13.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 21.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50024; SEA; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell junction; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Developmental protein; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..2104
FT                   /note="Transmembrane matrix receptor MUP-4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000423668"
FT   TOPO_DOM        16..1860
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1861..1881
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1882..2104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          71..110
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          122..163
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          175..213
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          220..265
FT                   /note="WR1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          278..315
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          327..360
FT                   /note="EGF-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          377..416
FT                   /note="EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          437..612
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          728..772
FT                   /note="EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          819..857
FT                   /note="EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          869..907
FT                   /note="EGF-like 9; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          919..958
FT                   /note="EGF-like 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          968..1007
FT                   /note="EGF-like 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1016..1058
FT                   /note="EGF-like 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1071..1110
FT                   /note="EGF-like 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1121..1160
FT                   /note="EGF-like 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1169..1208
FT                   /note="EGF-like 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1215..1254
FT                   /note="EGF-like 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1322..1444
FT                   /note="SEA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT   DOMAIN          1495..1620
FT                   /note="SEA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT   DOMAIN          1622..1658
FT                   /note="EGF-like 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1669..1705
FT                   /note="EGF-like 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1717..1754
FT                   /note="EGF-like 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1772..1810
FT                   /note="EGF-like 20; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1817..1853
FT                   /note="EGF-like 21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          2031..2104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2031..2053
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2057..2071
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2079..2096
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        556
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        879
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1037
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1730
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1782
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1838
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        83..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        126..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        136..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        179..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        186..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        282..294
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        288..303
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        331..344
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        338..353
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        355..359
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        381..395
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        389..404
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        732..746
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        740..756
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        758..771
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        823..836
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        830..845
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        873..886
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        880..895
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        923..937
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        931..946
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        972..985
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        979..995
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1020..1034
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1028..1046
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1075..1089
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1083..1098
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1125..1139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1133..1148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1173..1187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1181..1196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1219..1233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1227..1242
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1626..1637
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1631..1646
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1673..1687
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1681..1696
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1721..1733
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1727..1742
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1776..1789
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1783..1798
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1821..1830
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1824..1841
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1843..1852
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CONFLICT        919
FT                   /note="L -> P (in Ref. 1; AAK69172)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2104 AA;  230054 MW;  C98CD462CC434F8B CRC64;
     MRWVPLVLLP LIASAATTYQ HRQTYSSLQC RVNDPLSCNQ AKSEVCVFVN GQYRCECPVG
     VSRLADGRCL VVNECARPSL NACHKDAQCV DLAEGYTCRC NSGFADTSPD KVNKPGRQCQ
     KTTNECGAKQ TYGVDCDENA ACVDTPEGFQ CVCQPGYADV STSISKLPGR KCVESVNECT
     NGEADCSNNA DCFDRADGYE CKCRPGFVDA SPNVDKYPGR VCNKPKAPEY YGQQSRQPQC
     SEGSGCGPNE ECRFNTAGEK VCQCRRGSVQ QSNGVCKVFS QCEQANECDR NAFCSNTYDG
     PKCQCKDGFL DVSPDPVRLP GRKCQQVRNE CADGSHDCSH QAACQDTPTG YICSCNSNCI
     DVSSRYNLPP GRKCSVAANQ CSDKSLNSCD ENADCVQLPD GYTCKCFAGY VDVSSNANLP
     PGRVCTLSTA CPAQPTDLVF LIDGSGSIGS YVFQTEVLRF LAEFTELFDI APQKTRVSVV
     QYSDQIRHEF GLDNYSDRKS LQNAIRNIEY LTGLTRTGAA IEHVANEAFS ERRGARPVGQ
     VSRVAIVITD GRSQDNVTRP SDNARRQDIQ LFAVGVTNHV LDAELEEISG SKDRTFHVSG
     FEDLNTRLRS AIQRVACPHQ NNEDTYNKGP CDPSNHNGCD RSLNQVCQQK NGKFVCACPA
     GFDIHPVTKV CGGDICNPEI ATSCPDPEIC EKTPFGNWRC TCPADLGWRD RLTGVCKIGE
     KPVQTSESND ECSPNDVHSC PANSKCEKGA GGEFICKCDA GFQRNGRTNK CEAPGTCDPR
     MPDSCDARKK EKCLPDGRGA FACMCDRHHK RHPVTDICLI DECAAGVADC DPNAKCTDTD
     ESYICTCNEG FLDKSPEQNK KPGRVCSKQR NECLDGTHNC SMNADCIDLP DGFLCRCKED
     FVDISPNPNA FGGIDCRALV NECLITGGHN CHEHAICIDT RDSYKCQCKE GYVDHDELRN
     PGRTCKKLNQ ICESGKHECD KNARCVEKGA NDYECVCNAG FIDKSPLTHR PGRKCVEPIC
     SDDSKHDCHS AAICEENDSV PEKYTCKCRD GYLDVGAVMG GGKSGRECKE LVNECLSASL
     NSCDAAATCI DLDDGYTCKC PLGSKDESPV PKLPGRSCKG LVNECNIPHL NNCSHFATCI
     DLEEGYECKC KPEYHDQKPE QPGTECKFII NECLAENLND CSPNAMCIDK IDGYDCKCKA
     PFQDEMPSNP GRICRFDECA DPKDNDCDKH ALCIDTDDSY TCQCKEGFFD EISDPKKPGR
     VCIGLVIEPQ NQSEDPTTPD PNTIKCGNGL CHLDLGEVCV GGATCSCRPG ESRDNEKEKC
     VPTTSIPLVV RVMEYDGEPI QYRTDYSKPD TQAHIEIVDA VKKSVGKIIG KTDVAPRFVT
     TDVNYITNPK VQNSEWDKGL LGNVSVHLAG KEEVDKCRFY EQFAEIVREM GGRVDRIKLS
     DDADLDPCKK EEEKKGIPCG NTFCSIELGE ECIAGKICGC PKGQKRKDAN SPCRAVESWN
     LPLYVIRDGH EKITYSPSLS NPLNDDHKDL VSRFESGVAQ SYDKTPLKGA FVTAEVNEIE
     NPESRKKSWD TGILYNFTSH FVKGSVAEPA SVFTDLIDYI QKRNDFEVGK SKLFISPEQL
     NPFSNCYHSD CHPDAICKEV GKGYTCTCPD GFRDLNPSRP GRNCLSYRGV NECEKPELNE
     CSPHARCIDL DYLYKCECIR PYVNSAVGDA LPGSVCSIDY CQDVNYCPLN STCVNVDEQA
     RCDCKPGFVD LRKSGHLSEA GLGESICRRQ SDIDECALGL HNCSAAAICI DKKIGYECQC
     QEGYEDGNPS QPGRICAASL CGLCNGHGDC IHDALSSNVT CACLDGYTGQ FCETAPSNLP
     LILMTLLALL FLLLTLLCCL YMCARCRCFG ARGRSEGSAS GQEILGSDYY TIPRAKLARP
     LYGDEMGDDH AGALAAYLDD GASISSDGSI EEIERRVTTD VTTREVRTTT VRDDDGNIIS
     QSQTISHGNP HETDTEQYGM ISSDHYKTSA SEAMDAAMST SASGAAYNQS SGAMMSSASG
     HKSAYNQGYA SDSEDSDAGH AVYDRTTRTN QSHDFEPGAD PRTGTERSKR EFVTTTKAEE
     VNYF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025