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SI1L3_HUMAN
ID   SI1L3_HUMAN             Reviewed;        1781 AA.
AC   O60292; Q2TV87;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 3.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Signal-induced proliferation-associated 1-like protein 3;
DE            Short=SIPA1-like protein 3;
DE   AltName: Full=SPA-1-like protein 3;
GN   Name=SIPA1L3; Synonyms=KIAA0545, SPAL3;
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 [MRNA].
RA   Matsuura K., Kohu K., Akiyama T.;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-1781.
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   [4]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1544, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1699, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1448, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1364, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [10]
RP   INVOLVEMENT IN CTRCT45.
RX   PubMed=25804400; DOI=10.1038/ejhg.2015.46;
RA   Evers C., Paramasivam N., Hinderhofer K., Fischer C., Granzow M.,
RA   Schmidt-Bacher A., Eils R., Steinbeisser H., Schlesner M., Moog U.;
RT   "SIPA1L3 identified by linkage analysis and whole-exome sequencing as a
RT   novel gene for autosomal recessive congenital cataract.";
RL   Eur. J. Hum. Genet. 23:1627-1633(2015).
RN   [11]
RP   VARIANT TYR-148, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF
RP   VARIANT TYR-148, AND CHROMOSOMAL TRANSLOCATION.
RX   PubMed=26231217; DOI=10.1093/hmg/ddv298;
RA   Greenlees R., Mihelec M., Yousoof S., Speidel D., Wu S.K., Rinkwitz S.,
RA   Prokudin I., Perveen R., Cheng A., Ma A., Nash B., Gillespie R.,
RA   Loebel D.A., Clayton-Smith J., Lloyd I.C., Grigg J.R., Tam P.P., Yap A.S.,
RA   Becker T.S., Black G.C., Semina E., Jamieson R.V.;
RT   "Mutations in SIPA1L3 cause eye defects through disruption of cell polarity
RT   and cytoskeleton organization.";
RL   Hum. Mol. Genet. 24:5789-5804(2015).
CC   -!- FUNCTION: Plays a critical role in epithelial cell morphogenesis,
CC       polarity, adhesion and cytoskeletal organization in the lens
CC       (PubMed:26231217). {ECO:0000269|PubMed:26231217}.
CC   -!- INTERACTION:
CC       O60292; P63104: YWHAZ; NbExp=2; IntAct=EBI-2559690, EBI-347088;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:26231217}. Note=Detected in tricellular junctions.
CC       Colocalizes with apical F-actin. {ECO:0000269|PubMed:26231217}.
CC   -!- DISEASE: Note=A chromosomal translocation involving SIPA1L3 is found in
CC       a patient with bilateral severe ocular abnormalities including
CC       congenital cataracts, corneal clouding, iridocorneal and lenticular
CC       adhesions and microphthalmia. Chromosomal translocation
CC       t(2;19)(q37.3;q13.1). In addition to translocation, missense variant
CC       has been found in patient with bilateral congenital cataracts
CC       (PubMed:26231217). {ECO:0000269|PubMed:26231217}.
CC   -!- DISEASE: Cataract 45 (CTRCT45) [MIM:616851]: An opacification of the
CC       crystalline lens of the eye that frequently results in visual
CC       impairment or blindness. Opacities vary in morphology, are often
CC       confined to a portion of the lens, and may be static or progressive. In
CC       general, the more posteriorly located and dense an opacity, the greater
CC       the impact on visual function. {ECO:0000269|PubMed:25804400}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
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DR   EMBL; AY168880; AAO12531.1; -; mRNA.
DR   EMBL; AB011117; BAA25471.2; -; mRNA.
DR   EMBL; AC011465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS33007.1; -.
DR   RefSeq; NP_055888.1; NM_015073.2.
DR   RefSeq; XP_005258728.1; XM_005258671.4.
DR   RefSeq; XP_011524959.1; XM_011526657.2.
DR   RefSeq; XP_016882006.1; XM_017026517.1.
DR   AlphaFoldDB; O60292; -.
DR   SMR; O60292; -.
DR   BioGRID; 116722; 117.
DR   IntAct; O60292; 43.
DR   MINT; O60292; -.
DR   STRING; 9606.ENSP00000222345; -.
DR   iPTMnet; O60292; -.
DR   PhosphoSitePlus; O60292; -.
DR   BioMuta; SIPA1L3; -.
DR   EPD; O60292; -.
DR   jPOST; O60292; -.
DR   MassIVE; O60292; -.
DR   MaxQB; O60292; -.
DR   PaxDb; O60292; -.
DR   PeptideAtlas; O60292; -.
DR   PRIDE; O60292; -.
DR   ProteomicsDB; 49323; -.
DR   Antibodypedia; 59222; 71 antibodies from 21 providers.
DR   DNASU; 23094; -.
DR   Ensembl; ENST00000222345.11; ENSP00000222345.4; ENSG00000105738.11.
DR   GeneID; 23094; -.
DR   KEGG; hsa:23094; -.
DR   MANE-Select; ENST00000222345.11; ENSP00000222345.4; NM_015073.3; NP_055888.1.
DR   UCSC; uc002ohk.4; human.
DR   CTD; 23094; -.
DR   DisGeNET; 23094; -.
DR   GeneCards; SIPA1L3; -.
DR   HGNC; HGNC:23801; SIPA1L3.
DR   HPA; ENSG00000105738; Tissue enhanced (brain).
DR   MalaCards; SIPA1L3; -.
DR   MIM; 616655; gene.
DR   MIM; 616851; phenotype.
DR   neXtProt; NX_O60292; -.
DR   OpenTargets; ENSG00000105738; -.
DR   Orphanet; 98994; Total early-onset cataract.
DR   PharmGKB; PA134866783; -.
DR   VEuPathDB; HostDB:ENSG00000105738; -.
DR   eggNOG; KOG3686; Eukaryota.
DR   GeneTree; ENSGT00940000159183; -.
DR   HOGENOM; CLU_002127_0_0_1; -.
DR   InParanoid; O60292; -.
DR   OMA; WVQNGSM; -.
DR   OrthoDB; 28453at2759; -.
DR   PhylomeDB; O60292; -.
DR   TreeFam; TF318626; -.
DR   PathwayCommons; O60292; -.
DR   SignaLink; O60292; -.
DR   BioGRID-ORCS; 23094; 13 hits in 1076 CRISPR screens.
DR   ChiTaRS; SIPA1L3; human.
DR   GenomeRNAi; 23094; -.
DR   Pharos; O60292; Tbio.
DR   PRO; PR:O60292; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O60292; protein.
DR   Bgee; ENSG00000105738; Expressed in buccal mucosa cell and 186 other tissues.
DR   ExpressionAtlas; O60292; baseline and differential.
DR   Genevisible; O60292; HS.
DR   GO; GO:0045177; C:apical part of cell; IMP:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR   GO; GO:0061689; C:tricellular tight junction; IDA:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0003382; P:epithelial cell morphogenesis; IDA:UniProtKB.
DR   GO; GO:0090162; P:establishment of epithelial cell polarity; IDA:UniProtKB.
DR   GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.40.50.11210; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR035974; Rap/Ran-GAP_sf.
DR   InterPro; IPR000331; Rap/Ran_GAP_dom.
DR   InterPro; IPR031204; SIPA1L3.
DR   InterPro; IPR021818; SIPA1L_C.
DR   PANTHER; PTHR15711:SF15; PTHR15711:SF15; 1.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   Pfam; PF11881; SPAR_C; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF111347; SSF111347; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cataract; Cell membrane; Chromosomal rearrangement;
KW   Coiled coil; GTPase activation; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1781
FT                   /note="Signal-induced proliferation-associated 1-like
FT                   protein 3"
FT                   /id="PRO_0000056752"
FT   DOMAIN          611..828
FT                   /note="Rap-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT   DOMAIN          966..1042
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          45..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1046..1112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1124..1221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1236..1565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1583..1636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1685..1712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1720..1774
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        45..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1082..1112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1302..1324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1378..1392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1420..1451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1496..1523
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1527..1546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1387
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT   MOD_RES         1448
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1544
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1547
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT   MOD_RES         1619
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT   MOD_RES         1622
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT   MOD_RES         1677
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT   MOD_RES         1699
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1703
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT   VARIANT         148
FT                   /note="D -> Y (found in a patient with bilateral congenital
FT                   cataracts; unknown pathological significance; lack of
FT                   normal basal actin stress fiber formation; absence of
FT                   SIPA1L3 and F-actin colocalization; dbSNP:rs138476311)"
FT                   /evidence="ECO:0000269|PubMed:26231217"
FT                   /id="VAR_075045"
FT   VARIANT         1371
FT                   /note="G -> S (in dbSNP:rs2304133)"
FT                   /id="VAR_025476"
FT   VARIANT         1450
FT                   /note="P -> A (in dbSNP:rs3745945)"
FT                   /id="VAR_025477"
SQ   SEQUENCE   1781 AA;  194610 MW;  6A91F43B5BC3E175 CRC64;
     MTTYRAIPSD GVDLAASCGA RVGDVLPGPH TGDYAPLGFW AQNGSMSQPL GESPATATAT
     ATATTRPSPT TPAMPKMGVR ARVADWPPKR EALREHSNPS PSQDTDGTKA TKMAHSMRSI
     QNGQPPTSTP ASSGSKAFHR LSRRRSKDVE FQDGWPRSPG RAFLPLRHRS SSEITLSECD
     AEDAGEPRGA RHTGALPLFR EYGSTSSIDV QGMPEQSFFD ILNEFRSEQP DARGCQALTE
     LLRADPGPHL MGGGGGAKGD SHNGQPAKDS LLPLQPTKEK EKARKKPARG LGGGDTVDSS
     IFRKLRSSKP EGEAGRSPGE ADEGRSPPEA SRPWVCQKSF AHFDVQSMLF DLNEAAANRV
     SVSQRRNTTT GASAASAASA MASLTASRAH SLGGLDPAFT STEDLNCKEN LEQDLGDDNS
     NDLLLSCPHF RNEIGGECER NVSFSRASVG SPSSGEGHLA EPALSAYRTN ASISVLEVPK
     EQQRTQSRPR QYSIEHVDLG ARYYQDYFVG KEHANYFGVD EKLGPVAVSI KREKLEDHKE
     HGPQYQYRII FRTRELITLR GSILEDATPT ATKHGTGRGL PLKDALEYVI PELNIHCLRL
     ALNTPKVTEQ LLKLDEQGLC RKHKVGILYC KAGQSSEEEM YNNEEAGPAF EEFLSLIGEK
     VCLKGFTKYA AQLDVKTDST GTHSLYTMYQ DYEIMFHVST LLPYTPNNRQ QLLRKRHIGN
     DIVTIIFQEP GALPFTPKNI RSHFQHVFII VRVHNPCTDN VCYSMAVTRS KDAPPFGPPI
     PSGTTFRKSD VFRDFLLAKV INAENAAHKS DKFHTMATRT RQEYLKDLAE NCVSNTPIDS
     TGKFNLISLT SKKKEKTKAR AGAEQHSAGA IAWRVVAQDY AQGVEIDCIL GISNEFVVLL
     DLRTKEVVFN CYCGDVIGWT PDSSTLKIFY GRGDHIFLQA TEGSVEDIRE IVQRLKVMTS
     GWETVDMTLR RNGLGQLGFH VKYDGTVAEV EDYGFAWQAG LRQGSRLVEI CKVAVVTLTH
     DQMIDLLRTS VTVKVVIIPP FEDGTPRRGW PETYDMNTSE PKTEQESITP GGRPPYRSNA
     PWQWSGPASH NSLPASKWAT PTTPGHAQSL SRPLKQTPIV PFRESQPLHS KRPVSFPETP
     YTVSPAGADR VPPYRQPSGS FSTPGSATYV RYKPSPERYT AAPHPLLSLD PHFSHDGTSS
     GDSSSGGLTS QESTMERQKP EPLWHVPAQA RLSAIAGSSG NKHPSRQDAA GKDSPNRHSK
     GEPQYSSHSS SNTLSSNASS SHSDDRWFDP LDPLEPEQDP LSKGGSSDSG IDTTLYTSSP
     SCMSLAKAPR PAKPHKPPGS MGLCGGGREA AGRSHHADRR REVSPAPAVA GQSKGYRPKL
     YSSGSSTPTG LAGGSRDPPR QPSDMGSRVG YPAQVYKTAS AETPRPSQLA QPSPFQLSAS
     VPKSFFSKQP VRNKHPTGWK RTEEPPPRPL PFSDPKKQVD TNTKNVFGQP RLRASLRDLR
     SPRKNYKSTI EDDLKKLIIM DNLGPEQERD TGQSPQKGLQ RTLSDESLCS GRREPSFASP
     AGLEPGLPSD VLFTSTCAFP SSTLPARRQH QHPHPPVGPG ATPAAGSGFP EKKSTISASE
     LSLADGRDRP LRRLDPGLMP LPDTAAGLEW SSLVNAAKAY EVQRAVSLFS LNDPALSPDI
     PPAHSPVHSH LSLERGPPTP RTTPTMSEEP PLDLTGKVYQ LEVMLKQLHT DLQKEKQDKV
     VLQSEVASLR QNNQRLQEES QAASEQLRKF AEIFCREKKE L
 
 
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