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ATL2_HUMAN
ID   ATL2_HUMAN              Reviewed;         951 AA.
AC   Q86TH1; B1B0D5; O60345;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=ADAMTS-like protein 2;
DE            Short=ADAMTSL-2;
DE   Flags: Precursor;
GN   Name=ADAMTSL2; Synonyms=KIAA0605;
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 [LARGE SCALE MRNA], AND VARIANT ILE-364.
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PNS;
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   [4]
RP   GLYCOSYLATION AT ASN-428.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [5]
RP   VARIANTS GPHYSD1 HIS-113; LYS-114; LEU-147 AND ARG-811, CHARACTERIZATION OF
RP   VARIANTS HIS-113; LEU-147 AND ARG-811, AND INTERACTION WITH LTBP1.
RX   PubMed=18677313; DOI=10.1038/ng.199;
RA   Le Goff C., Morice-Picard F., Dagoneau N., Wang L.W., Perrot C., Crow Y.J.,
RA   Bauer F., Flori E., Prost-Squarcioni C., Krakow D., Ge G., Greenspan D.S.,
RA   Bonnet D., Le Merrer M., Munnich A., Apte S.S., Cormier-Daire V.;
RT   "ADAMTSL2 mutations in geleophysic dysplasia demonstrate a role for ADAMTS-
RT   like proteins in TGF-beta bioavailability regulation.";
RL   Nat. Genet. 40:1119-1123(2008).
RN   [6]
RP   VARIANTS GPHYSD1 CYS-50; GLN-72; LYS-114; TRP-159; THR-165; ARG-171;
RP   CYS-221; THR-239; 383-ASN--ASP-392 DEL; CYS-593; LEU-635 AND LEU-906.
RX   PubMed=21415077; DOI=10.1136/jmg.2010.087544;
RA   Allali S., Le Goff C., Pressac-Diebold I., Pfennig G., Mahaut C.,
RA   Dagoneau N., Alanay Y., Brady A.F., Crow Y.J., Devriendt K.,
RA   Drouin-Garraud V., Flori E., Genevieve D., Hennekam R.C., Hurst J.,
RA   Krakow D., Le Merrer M., Lichtenbelt K.D., Lynch S.A., Lyonnet S.,
RA   MacDermot K., Mansour S., Megarbane A., Santos H.G., Splitt M.,
RA   Superti-Furga A., Unger S., Williams D., Munnich A., Cormier-Daire V.;
RT   "Molecular screening of ADAMTSL2 gene in 33 patients reveals the genetic
RT   heterogeneity of geleophysic dysplasia.";
RL   J. Med. Genet. 48:417-421(2011).
CC   -!- SUBUNIT: Interacts with LTBP1. {ECO:0000269|PubMed:18677313}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Glycosylated (By similarity). Can be O-fucosylated by POFUT2 on a
CC       serine or a threonine residue found within the consensus sequence C1-
CC       X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
CC       the first and second cysteine residue of the repeat, respectively.
CC       Fucosylated repeats can then be further glycosylated by the addition of
CC       a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL.
CC       Fucosylation mediates the efficient secretion of ADAMTS family members.
CC       Can also be C-glycosylated with one or two mannose molecules on
CC       tryptophan residues within the consensus sequence W-X-X-W of the TPRs,
CC       and N-glycosylated. These other glycosylations can also facilitate
CC       secretion (By similarity). {ECO:0000250}.
CC   -!- DISEASE: Geleophysic dysplasia 1 (GPHYSD1) [MIM:231050]: An autosomal
CC       recessive disorder characterized by severe short stature, short hands
CC       and feet, joint limitations, and skin thickening. Radiologic features
CC       include delayed bone age, cone-shaped epiphyses, shortened long tubular
CC       bones, and ovoid vertebral bodies. Affected individuals have
CC       characteristic facial features including a 'happy' face with full
CC       cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin
CC       upper lip. Other distinctive features include progressive cardiac
CC       valvular thickening often leading to an early death, toe walking,
CC       tracheal stenosis, respiratory insufficiency, and lysosomal-like
CC       storage vacuoles in various tissues. {ECO:0000269|PubMed:18677313,
CC       ECO:0000269|PubMed:21415077}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: There is a significant increase in total and active
CC       TGFB1 in the culture medium as well as nuclear localization of
CC       phosphorylated SMAD2 in fibroblasts from individuals with geleophysic
CC       dysplasia.
CC   -!- CAUTION: Although strongly similar to members of the ADAMTS family it
CC       lacks the metalloprotease and disintegrin-like domains which are
CC       typical of that family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA25531.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB011177; BAA25531.2; ALT_INIT; mRNA.
DR   EMBL; BX324209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX649571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX629352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC050544; AAH50544.1; -; mRNA.
DR   CCDS; CCDS6976.1; -.
DR   PIR; T00260; T00260.
DR   RefSeq; NP_001138792.1; NM_001145320.1.
DR   RefSeq; NP_055509.2; NM_014694.3.
DR   RefSeq; XP_005272296.1; XM_005272239.2.
DR   AlphaFoldDB; Q86TH1; -.
DR   SMR; Q86TH1; -.
DR   BioGRID; 115068; 2.
DR   IntAct; Q86TH1; 3.
DR   MINT; Q86TH1; -.
DR   STRING; 9606.ENSP00000346478; -.
DR   GlyConnect; 1911; 5 N-Linked glycans (4 sites).
DR   GlyGen; Q86TH1; 15 sites, 6 N-linked glycans (4 sites), 2 O-linked glycans (4 sites).
DR   iPTMnet; Q86TH1; -.
DR   PhosphoSitePlus; Q86TH1; -.
DR   BioMuta; ADAMTSL2; -.
DR   DMDM; 74750384; -.
DR   jPOST; Q86TH1; -.
DR   MassIVE; Q86TH1; -.
DR   PaxDb; Q86TH1; -.
DR   PeptideAtlas; Q86TH1; -.
DR   PRIDE; Q86TH1; -.
DR   ProteomicsDB; 69695; -.
DR   Antibodypedia; 45302; 87 antibodies from 24 providers.
DR   DNASU; 9719; -.
DR   Ensembl; ENST00000354484.8; ENSP00000346478.4; ENSG00000197859.11.
DR   Ensembl; ENST00000393060.1; ENSP00000376780.1; ENSG00000197859.11.
DR   Ensembl; ENST00000651351.2; ENSP00000498961.2; ENSG00000197859.11.
DR   GeneID; 9719; -.
DR   KEGG; hsa:9719; -.
DR   MANE-Select; ENST00000651351.2; ENSP00000498961.2; NM_014694.4; NP_055509.2.
DR   UCSC; uc011mdl.2; human.
DR   CTD; 9719; -.
DR   DisGeNET; 9719; -.
DR   GeneCards; ADAMTSL2; -.
DR   GeneReviews; ADAMTSL2; -.
DR   HGNC; HGNC:14631; ADAMTSL2.
DR   HPA; ENSG00000197859; Tissue enhanced (heart muscle, liver).
DR   MalaCards; ADAMTSL2; -.
DR   MIM; 231050; phenotype.
DR   MIM; 612277; gene.
DR   neXtProt; NX_Q86TH1; -.
DR   OpenTargets; ENSG00000197859; -.
DR   Orphanet; 1901; Dermatosparaxis Ehlers-Danlos syndrome.
DR   Orphanet; 2623; Geleophysic dysplasia.
DR   PharmGKB; PA134920655; -.
DR   VEuPathDB; HostDB:ENSG00000197859; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000159447; -.
DR   HOGENOM; CLU_000660_6_1_1; -.
DR   InParanoid; Q86TH1; -.
DR   OrthoDB; 807790at2759; -.
DR   PhylomeDB; Q86TH1; -.
DR   TreeFam; TF316874; -.
DR   PathwayCommons; Q86TH1; -.
DR   Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR   Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR   SignaLink; Q86TH1; -.
DR   BioGRID-ORCS; 9719; 11 hits in 1064 CRISPR screens.
DR   ChiTaRS; ADAMTSL2; human.
DR   GenomeRNAi; 9719; -.
DR   Pharos; Q86TH1; Tbio.
DR   PRO; PR:Q86TH1; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q86TH1; protein.
DR   Bgee; ENSG00000197859; Expressed in right atrium auricular region and 92 other tissues.
DR   ExpressionAtlas; Q86TH1; baseline and differential.
DR   Genevisible; Q86TH1; HS.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050436; F:microfibril binding; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0060481; P:lobar bronchus epithelium development; IEA:Ensembl.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR   Gene3D; 2.20.100.10; -; 5.
DR   InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR   InterPro; IPR010294; ADAMTS_spacer1.
DR   InterPro; IPR010909; PLAC.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   Pfam; PF05986; ADAM_spacer1; 1.
DR   Pfam; PF08686; PLAC; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00209; TSP1; 7.
DR   SUPFAM; SSF82895; SSF82895; 7.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 4.
PE   1: Evidence at protein level;
KW   Disease variant; Disulfide bond; Dwarfism; Glycoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..951
FT                   /note="ADAMTS-like protein 2"
FT                   /id="PRO_0000249682"
FT   DOMAIN          47..106
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          564..618
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          622..686
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          688..736
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          737..795
FT                   /note="TSP type-1 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          797..851
FT                   /note="TSP type-1 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          853..908
FT                   /note="TSP type-1 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          912..950
FT                   /note="PLAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT   REGION          414..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19139490"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        533
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        544
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        731
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        807
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        59..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        63..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        74..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   VARIANT         50
FT                   /note="W -> C (in GPHYSD1; dbSNP:rs1395219766)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066543"
FT   VARIANT         72
FT                   /note="R -> Q (in GPHYSD1; dbSNP:rs387907064)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066544"
FT   VARIANT         113
FT                   /note="R -> H (in GPHYSD1; leads to the reduced secretion
FT                   of the mutated protein; dbSNP:rs113994122)"
FT                   /evidence="ECO:0000269|PubMed:18677313"
FT                   /id="VAR_054874"
FT   VARIANT         114
FT                   /note="E -> K (in GPHYSD1; dbSNP:rs113994123)"
FT                   /evidence="ECO:0000269|PubMed:18677313,
FT                   ECO:0000269|PubMed:21415077"
FT                   /id="VAR_054875"
FT   VARIANT         147
FT                   /note="P -> L (in GPHYSD1; leads to the reduced secretion
FT                   of the mutated protein; dbSNP:rs113994121)"
FT                   /evidence="ECO:0000269|PubMed:18677313"
FT                   /id="VAR_054876"
FT   VARIANT         159
FT                   /note="R -> W (in GPHYSD1; dbSNP:rs776178041)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066545"
FT   VARIANT         165
FT                   /note="A -> T (in GPHYSD1; dbSNP:rs764516811)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066546"
FT   VARIANT         171
FT                   /note="C -> R (in GPHYSD1)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066547"
FT   VARIANT         221
FT                   /note="R -> C (in GPHYSD1; dbSNP:rs387907065)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066548"
FT   VARIANT         239
FT                   /note="A -> T (in GPHYSD1)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066549"
FT   VARIANT         364
FT                   /note="V -> I (in dbSNP:rs35767802)"
FT                   /evidence="ECO:0000269|PubMed:9628581"
FT                   /id="VAR_046011"
FT   VARIANT         383..392
FT                   /note="Missing (in GPHYSD1)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066550"
FT   VARIANT         593
FT                   /note="R -> C (in GPHYSD1)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066551"
FT   VARIANT         635
FT                   /note="S -> L (in GPHYSD1)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066552"
FT   VARIANT         811
FT                   /note="G -> R (in GPHYSD1; leads to the reduced secretion
FT                   of the mutated protein; dbSNP:rs113994124)"
FT                   /evidence="ECO:0000269|PubMed:18677313"
FT                   /id="VAR_054877"
FT   VARIANT         906
FT                   /note="P -> L (in GPHYSD1; dbSNP:rs969732840)"
FT                   /evidence="ECO:0000269|PubMed:21415077"
FT                   /id="VAR_066553"
FT   CONFLICT        59
FT                   /note="C -> F (in Ref. 1; BAA25531)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   951 AA;  104621 MW;  93A9B0DC5BAB6CC7 CRC64;
     MDGRWQCSCW AWFLLVLAVV AGDTVSTGST DNSPTSNSLE GGTDATAFWW GEWTKWTACS
     RSCGGGVTSQ ERHCLQQRRK SVPGPGNRTC TGTSKRYQLC RVQECPPDGR SFREEQCVSF
     NSHVYNGRTH QWKPLYPDDY VHISSKPCDL HCTTVDGQRQ LMVPARDGTS CKLTDLRGVC
     VSGKCEPIGC DGVLFSTHTL DKCGICQGDG SSCTHVTGNY RKGNAHLGYS LVTHIPAGAR
     DIQIVERKKS ADVLALADEA GYYFFNGNYK VDSPKNFNIA GTVVKYRRPM DVYETGIEYI
     VAQGPTNQGL NVMVWNQNGK SPSITFEYTL LQPPHESRPQ PIYYGFSESA ESQGLDGAGL
     MGFVPHNGSL YGQASSERLG LDNRLFGHPG LDMELGPSQG QETNEVCEQA GGGACEGPPR
     GKGFRDRNVT GTPLTGDKDD EEVDTHFASQ EFFSANAISD QLLGAGSDLK DFTLNETVNS
     IFAQGAPRSS LAESFFVDYE ENEGAGPYLL NGSYLELSSD RVANSSSEAP FPNVSTSLLT
     SAGNRTHKAR TRPKARKQGV SPADMYRWKL SSHEPCSATC TTGVMSAYAM CVRYDGVEVD
     DSYCDALTRP EPVHEFCAGR ECQPRWETSS WSECSRTCGE GYQFRVVRCW KMLSPGFDSS
     VYSDLCEAAE AVRPEERKTC RNPACGPQWE MSEWSECTAK CGERSVVTRD IRCSEDEKLC
     DPNTRPVGEK NCTGPPCDRQ WTVSDWGPCS GSCGQGRTIR HVYCKTSDGR VVPESQCQME
     TKPLAIHPCG DKNCPAHWLA QDWERCNTTC GRGVKKRLVL CMELANGKPQ TRSGPECGLA
     KKPPEESTCF ERPCFKWYTS PWSECTKTCG VGVRMRDVKC YQGTDIVRGC DPLVKPVGRQ
     ACDLQPCPTE PPDDSCQDQP GTNCALAIKV NLCGHWYYSK ACCRSCRPPH S
 
 
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