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CO4A4_MOUSE
ID   CO4A4_MOUSE             Reviewed;        1682 AA.
AC   Q9QZR9; Q149M2; Q64457;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Collagen alpha-4(IV) chain;
DE   Flags: Precursor;
GN   Name=Col4a4 {ECO:0000312|MGI:MGI:104687};
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] {ECO:0000305, ECO:0000312|EMBL:AAD50450.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic kidney {ECO:0000312|EMBL:AAD50450.1};
RX   PubMed=10534397; DOI=10.1006/geno.1999.5943;
RA   Lu W., Phillips C.L., Killen P.D., Hlaing T., Harrison W.R., Elder F.F.B.,
RA   Miner J.H., Overbeek P.A., Meisler M.H.;
RT   "Insertional mutation of the collagen genes Col4a3 and Col4a4 in a mouse
RT   model of Alport syndrome.";
RL   Genomics 61:113-124(1999).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAI17710.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [3] {ECO:0000305, ECO:0000312|EMBL:CAA84530.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1371-1682 (ISOFORM 1), FUNCTION, ASSOCIATED
RP   WITH LAMB2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ {ECO:0000312|EMBL:CAA84530.1};
RC   TISSUE=Kidney {ECO:0000312|EMBL:CAA84530.1};
RX   PubMed=7962065; DOI=10.1083/jcb.127.3.879;
RA   Miner J.H., Sanes J.R.;
RT   "Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae:
RT   sequence, distribution, association with laminins, and developmental
RT   switches.";
RL   J. Cell Biol. 127:879-891(1994).
RN   [4] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=10639489; DOI=10.1177/002215540004800208;
RA   Miosge N., Quondamatteo F., Klenczar C., Herken R.;
RT   "Nidogen-1. Expression and ultrastructural localization during the onset of
RT   mesoderm formation in the early mouse embryo.";
RL   J. Histochem. Cytochem. 48:229-238(2000).
RN   [5] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12225806; DOI=10.1016/s0945-053x(02)00014-8;
RA   Kelley P.B., Sado Y., Duncan M.K.;
RT   "Collagen IV in the developing lens capsule.";
RL   Matrix Biol. 21:415-423(2002).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023;
RA   Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y.,
RA   Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C.,
RA   Lako M.;
RT   "Extracellular matrix component expression in human pluripotent stem cell-
RT   derived retinal organoids recapitulates retinogenesis in vivo and reveals
RT   an important role for IMPG1 and CD44 in the development of photoreceptors
RT   and interphotoreceptor matrix.";
RL   Acta Biomater. 74:207-221(2018).
CC   -!- FUNCTION: Type IV collagen is the major structural component of
CC       glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork
CC       together with laminins, proteoglycans and entactin/nidogen.
CC       {ECO:0000250|UniProtKB:P53420, ECO:0000269|PubMed:10639489,
CC       ECO:0000269|PubMed:7962065}.
CC   -!- SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha
CC       6(IV), each of which can form a triple helix structure with 2 other
CC       chains to generate type IV collagen network. The alpha 3(IV) chain
CC       forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this
CC       triple helical structure dimerizes through NC1-NC1 domain interactions
CC       such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one
CC       protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV)
CC       chains of the opposite protomer, respectively (By similarity).
CC       Associates with LAMB2 at the neuromuscular junction and in GBM.
CC       {ECO:0000250|UniProtKB:P53420, ECO:0000269|PubMed:7962065}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736,
CC       ECO:0000269|PubMed:7962065}. Note=Colocalizes with COL4A3 and COL4A5 in
CC       GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL).
CC       {ECO:0000250|UniProtKB:P53420, ECO:0000269|PubMed:7962065}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:10534397, ECO:0000269|PubMed:7962065};
CC         IsoId=Q9QZR9-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15489334};
CC         IsoId=Q9QZR9-2; Sequence=VSP_052356, VSP_052357;
CC   -!- TISSUE SPECIFICITY: Expressed in Bruch's membrane, outer plexiform
CC       layer, inner nuclear layer, inner plexiform layer, ganglion cell layer,
CC       inner limiting membrane and around the blood vessels of the retina (at
CC       protein level) (PubMed:29777959). Highly expressed in kidney and lung
CC       (PubMed:7962065). Detected at lower levels in heart, muscle and skin
CC       (PubMed:7962065). {ECO:0000269|PubMed:29777959,
CC       ECO:0000269|PubMed:7962065}.
CC   -!- DEVELOPMENTAL STAGE: The expression of collagen IV undergoes a
CC       developmental shift in the developing lens capsule. During the early
CC       stages of lens capsule development expression of collagens alpha 1(IV),
CC       alpha 2(IV), alpha 5(IV) and alpha 6(IV) is observed; this is
CC       consistent with the presence of fibrillar alpha 1(IV)-alpha 1(IV)-alpha
CC       2(IV) protomers and of elastic alpha 5(IV)-alpha 5(IV)-alpha 6(IV)
CC       protomers. In the later stages of development components of the more
CC       cross-linked alpha 3(IV)-alpha 4(IV)-alpha 5(IV) protomer appear.
CC       {ECO:0000269|PubMed:12225806}.
CC   -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain
CC       (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats
CC       in the long central triple-helical domain (which may cause flexibility
CC       in the triple helix), and a short N-terminal triple-helical 7S domain.
CC       {ECO:0000250|UniProtKB:P53420, ECO:0000255|PROSITE-ProRule:PRU00736}.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC       (G-X-Y) are hydroxylated in some or all of the chains.
CC       {ECO:0000250|UniProtKB:P53420, ECO:0000255|PROSITE-ProRule:PRU00736}.
CC   -!- PTM: Type IV collagens contain numerous cysteine residues which are
CC       involved in inter- and intramolecular disulfide bonding. 12 of these,
CC       located in the NC1 domain, are conserved in all known type IV
CC       collagens. {ECO:0000250|UniProtKB:P53420, ECO:0000255|PROSITE-
CC       ProRule:PRU00736}.
CC   -!- PTM: The trimeric structure of the NC1 domains is stabilized by
CC       covalent bonds between Lys and Met residues. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The kidneys of transgenic mice where the 5' portions of
CC       both COL4A3 and COL4A4 and the shared intergenic promoter region were
CC       deleted exhibit morphological and ultrastructural features
CC       characteristic of the human hereditary disorder Alport syndrome,
CC       including disorganization and multilamellar structure of the GBM and
CC       delayed onset glomerulonephritis. {ECO:0000269|PubMed:10534397}.
CC   -!- SIMILARITY: Belongs to the type IV collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00736}.
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DR   EMBL; AF169388; AAD50450.1; -; mRNA.
DR   EMBL; BC117709; AAI17710.1; -; mRNA.
DR   EMBL; Z35167; CAA84530.1; -; mRNA.
DR   CCDS; CCDS35630.1; -. [Q9QZR9-1]
DR   PIR; I48303; I48303.
DR   RefSeq; NP_031761.1; NM_007735.2. [Q9QZR9-1]
DR   AlphaFoldDB; Q9QZR9; -.
DR   BioGRID; 198819; 1.
DR   ComplexPortal; CPX-2961; Collagen type IV trimer variant 3.
DR   STRING; 10090.ENSMUSP00000084282; -.
DR   GlyGen; Q9QZR9; 3 sites.
DR   iPTMnet; Q9QZR9; -.
DR   PhosphoSitePlus; Q9QZR9; -.
DR   MaxQB; Q9QZR9; -.
DR   PaxDb; Q9QZR9; -.
DR   PRIDE; Q9QZR9; -.
DR   ProteomicsDB; 279130; -. [Q9QZR9-1]
DR   ProteomicsDB; 279131; -. [Q9QZR9-2]
DR   Antibodypedia; 54339; 138 antibodies from 23 providers.
DR   DNASU; 12829; -.
DR   Ensembl; ENSMUST00000087050; ENSMUSP00000084282; ENSMUSG00000067158. [Q9QZR9-1]
DR   GeneID; 12829; -.
DR   KEGG; mmu:12829; -.
DR   UCSC; uc033fjy.1; mouse. [Q9QZR9-1]
DR   CTD; 1286; -.
DR   MGI; MGI:104687; Col4a4.
DR   VEuPathDB; HostDB:ENSMUSG00000067158; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000153991; -.
DR   HOGENOM; CLU_002023_1_0_1; -.
DR   InParanoid; Q9QZR9; -.
DR   OMA; KGFPGCD; -.
DR   OrthoDB; 63831at2759; -.
DR   PhylomeDB; Q9QZR9; -.
DR   TreeFam; TF344135; -.
DR   Reactome; R-MMU-1442490; Collagen degradation.
DR   Reactome; R-MMU-1474244; Extracellular matrix organization.
DR   Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-MMU-186797; Signaling by PDGF.
DR   Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   Reactome; R-MMU-2214320; Anchoring fibril formation.
DR   Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR   Reactome; R-MMU-3000157; Laminin interactions.
DR   Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-MMU-419037; NCAM1 interactions.
DR   Reactome; R-MMU-8948216; Collagen chain trimerization.
DR   BioGRID-ORCS; 12829; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Col4a4; mouse.
DR   PRO; PR:Q9QZR9; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9QZR9; protein.
DR   Bgee; ENSMUSG00000067158; Expressed in epithelium of lens and 90 other tissues.
DR   Genevisible; Q9QZR9; MM.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0005587; C:collagen type IV trimer; IDA:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IPI:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0032836; P:glomerular basement membrane development; IMP:MGI.
DR   Gene3D; 2.170.240.10; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR001442; Collagen_IV_NC.
DR   InterPro; IPR036954; Collagen_IV_NC_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF01413; C4; 2.
DR   Pfam; PF01391; Collagen; 15.
DR   SMART; SM00111; C4; 2.
DR   SUPFAM; SSF56436; SSF56436; 2.
DR   PROSITE; PS51403; NC1_IV; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Basement membrane; Collagen; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..1682
FT                   /note="Collagen alpha-4(IV) chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283793"
FT   DOMAIN          1457..1682
FT                   /note="Collagen IV NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   REGION          31..56
FT                   /note="7S domain"
FT                   /evidence="ECO:0000250|UniProtKB:P53420"
FT   REGION          56..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..1451
FT                   /note="Triple-helical region"
FT                   /evidence="ECO:0000250|UniProtKB:P53420"
FT   REGION          379..1453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           86..88
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           137..139
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           181..183
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           587..589
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           593..595
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           716..718
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           980..982
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           992..994
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           1144..1146
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        379..412
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..443
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..501
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..539
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..636
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..931
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1026
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1210..1236
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1270
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1290..1305
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1321..1338
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1378
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            1197..1198
FT                   /note="Cleavage; by collagenase"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        661
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1472..1561
FT                   /note="Or C-1472 with C-1558"
FT                   /evidence="ECO:0000250|UniProtKB:P53420,
FT                   ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1505..1558
FT                   /note="Or C-1505 with C-1561"
FT                   /evidence="ECO:0000250|UniProtKB:P53420,
FT                   ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1517..1523
FT                   /evidence="ECO:0000250|UniProtKB:P53420,
FT                   ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1580..1678
FT                   /note="Or C-1580 with C-1675"
FT                   /evidence="ECO:0000250|UniProtKB:P53420,
FT                   ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1614..1675
FT                   /note="Or C-1614 with C-1678"
FT                   /evidence="ECO:0000250|UniProtKB:P53420,
FT                   ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1626..1633
FT                   /evidence="ECO:0000250|UniProtKB:P53420,
FT                   ECO:0000255|PROSITE-ProRule:PRU00736"
FT   VAR_SEQ         470..488
FT                   /note="GRRGAKGAKGNKGLCTCPP -> PLWIKQTLYMWSCSPFSFY (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_052356"
FT   VAR_SEQ         489..1682
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_052357"
FT   CONFLICT        1373
FT                   /note="L -> F (in Ref. 3; CAA84530)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1654
FT                   /note="A -> P (in Ref. 3; CAA84530)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1682 AA;  164096 MW;  6F7B679EDD76E904 CRC64;
     MRCFFRWTKS FVTAPWSLIF ILFTIQYEYG SGKKYGGPCG GRNCSVCQCF PEKGSRGHPG
     PLGPQGPIGP LGPLGPIGIP GEKGERGDSG SPGPPGEKGD KGPTGVPGFP GVDGVPGHPG
     PPGPRGKPGV DGYNGSRGDP GYPGERGAPG PGGPPGQPGE NGEKGRSVYI TGGVKGIQGD
     RGDPGPPGLP GSRGAQGSPG PMGHAGAPGL AGPIGHPGSP GLKGNPATGL KGQRGEPGEV
     GQRGPPGPTL LVQPPDLSIY KGEKGVKGMP GMIGPPGPPG RKGAPGVGIK GEKGIPGFPG
     PRGEPGSHGP PGFPGFKGIQ GAAGEPGLFG FLGPKGDLGD RGYPGPPGIL LTPAPPLKGV
     PGDPGPPGYY GEIGDVGLPG PPGPPGRPGE TCPGMMGPPG PPGVPGPPGF PGEAGVPGRL
     DCAPGKPGKP GLPGLPGAPG PEGPPGSDVI YCRPGCPGPM GEKGKVGPPG RRGAKGAKGN
     KGLCTCPPGP MGPPGPPGPP GRQGSKGDLG LPGWHGEKGD PGQPGAEGPP GPPGRPGAMG
     PPGHKGEKGD MVISRVKGQK GERGLDGPPG FPGPHGQDGG DGRPGERGDP GPRGDHKDAA
     PGERGLPGLP GPPGRTGPEG PPGLGFPGPP GQRGLPGEPG RPGTRGFDGT KGQKGDSILC
     NVSYPGKPGL PGLDGPPGLK GFPGPPGAPG MRCPDGQKGQ RGKPGMSGIP GPPGFRGDMG
     DPGIKGEKGT SPIGPPGPPG SPGKDGQKGI PGDPAFGDPG PPGERGLPGA PGMKGQKGHP
     GCPGAGGPPG IPGSPGLKGP KGREGSRGFP GIPGSPGHSC ERGAPGIPGQ PGLPGTPGDP
     GAPGWKGQPG DMGPSGPAGM KGLPGLPGLP GADGLRGPPG IPGPNGEDGL PGLPGLKGLP
     GLPGFPGFPG ERGKPGPDGE PGRKGEVGEK GWPGLKGDLG ERGAKGDRGL PGDAGEAVTS
     RKGEPGDAGP PGDGGFSGER GDKGSSGMRG GRGDPGRDGL PGLHRGQPGI DGPPGPPGPP
     GPPGSPGLRG VIGFPGFPGD QGDPGSPGPP GFPGDDGARG PKGYKGDPAS QCGPPGPKGE
     PGSPGYQGRT GVPGEKGFPG DEGPRGPPGR PGQPGSFGPP GCPGDPGMPG LKGHPGEVGD
     PGPRGDAGDF GRPGPAGVKG PLGSPGLNGL HGLKGEKGTK GASGLLEMGP PGPMGMPGQK
     GEKGDPGSPG ISPPGLPGEK GFPGPPGRPG PPGPAGAPGR AAKGDIPDPG PPGDRGPPGP
     DGPRGVPGPP GSPGNVDLLK GDPGDCGLPG PPGSRGPPGP PGCQGPPGCD GKDGQKGPMG
     LPGLPGPPGL PGAPGEKGLP GPPGRKGPVG PPGCRGEPGP PADVDSCPRI PGLPGVPGPR
     GPEGAMGEPG RRGLPGPGCK GEPGPDGRRG QDGIPGSPGP PGRKGDTGEA GCPGAPGPPG
     PTGDPGPKGF GPGSLSGFLL VLHSQTDQEP ACPVGMPRLW TGYSLLYMEG QEKAHNQDLG
     LAGSCLPVFS TLPFAYCNIH QVCHYAQRND RSYWLSSAAP LPMMPLSEEE IRSYISRCAV
     CEAPAQAVAV HSQDQSIPPC PRTWRSLWIG YSFLMHTGAG DQGGGQALMS PGSCLEDFRA
     APFVECQGRQ GTCHFFANEY SFWLTTVNPD LQFASGPSPD TLKEVQAQRR KISRCQVCMK
     HS
 
 
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