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ASTN1_HUMAN
ID   ASTN1_HUMAN             Reviewed;        1302 AA.
AC   O14525; A5PL12; B4DHI9; E9PFR8; O60799; Q5W0V7; Q5W0V8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 3.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=Astrotactin-1;
DE   Flags: Precursor;
GN   Name=ASTN1; Synonyms=ASTN, KIAA0289;
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] (ISOFORM 1), AND VARIANTS ARG-932
RP   AND GLN-942.
RC   TISSUE=Brain;
RX   PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA   Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA   Nomura N.;
RT   "Construction and characterization of human brain cDNA libraries suitable
RT   for analysis of cDNA clones encoding relatively large proteins.";
RL   DNA Res. 4:53-59(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ARG-932
RP   AND GLN-942.
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ARG-932
RP   AND GLN-942.
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).
CC   -!- FUNCTION: Neuronal adhesion molecule that is required for normal
CC       migration of young postmitotic neuroblasts along glial fibers,
CC       especially in the cerebellum. Required for normal rate of migration of
CC       granule cells during brain development and for normal cerebellum
CC       development. {ECO:0000250|UniProtKB:Q61137}.
CC   -!- SUBUNIT: Interacts with ASTN2; the interaction is not calcium-
CC       dependent. {ECO:0000250|UniProtKB:Q61137}.
CC   -!- INTERACTION:
CC       O14525-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-21977454, EBI-742054;
CC       O14525-2; Q14145: KEAP1; NbExp=4; IntAct=EBI-21977454, EBI-751001;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q61137};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q61137}. Perikaryon
CC       {ECO:0000250|UniProtKB:Q61137}. Endosome
CC       {ECO:0000250|UniProtKB:Q61137}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle {ECO:0000250|UniProtKB:Q61137}. Note=Detected close to the
CC       anterior pole and at the base of the leading process in migrating
CC       neurons. Is internalized from the membrane via clathrin-coated vesicles
CC       and endosomes, and recycled to the anterior pole of the migrating cell.
CC       {ECO:0000250|UniProtKB:Q61137}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2;
CC         IsoId=O14525-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=O14525-2; Sequence=VSP_001371;
CC       Name=3;
CC         IsoId=O14525-3; Sequence=VSP_001371, VSP_045069;
CC   -!- SIMILARITY: Belongs to the astrotactin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA22958.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB006627; BAA22958.1; ALT_INIT; mRNA.
DR   EMBL; AK295126; BAG58151.1; -; mRNA.
DR   EMBL; AL021398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL022145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL031290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW91007.1; -; Genomic_DNA.
DR   EMBL; BC142697; AAI42698.1; -; mRNA.
DR   CCDS; CCDS1319.1; -. [O14525-2]
DR   CCDS; CCDS44280.1; -. [O14525-3]
DR   PIR; T00038; T00038.
DR   RefSeq; NP_996991.1; NM_207108.2. [O14525-3]
DR   RefSeq; XP_016856829.1; XM_017001340.1.
DR   AlphaFoldDB; O14525; -.
DR   SMR; O14525; -.
DR   BioGRID; 106952; 6.
DR   IntAct; O14525; 6.
DR   STRING; 9606.ENSP00000354536; -.
DR   TCDB; 9.B.87.2.1; the selenoprotein p receptor (selp-receptor) family.
DR   GlyGen; O14525; 6 sites.
DR   iPTMnet; O14525; -.
DR   PhosphoSitePlus; O14525; -.
DR   BioMuta; ASTN1; -.
DR   EPD; O14525; -.
DR   MassIVE; O14525; -.
DR   PaxDb; O14525; -.
DR   PeptideAtlas; O14525; -.
DR   PRIDE; O14525; -.
DR   ProteomicsDB; 20161; -.
DR   ProteomicsDB; 48071; -. [O14525-1]
DR   ProteomicsDB; 48072; -. [O14525-2]
DR   Antibodypedia; 55629; 20 antibodies from 12 providers.
DR   DNASU; 460; -.
DR   Ensembl; ENST00000361833.7; ENSP00000354536.2; ENSG00000152092.16. [O14525-2]
DR   Ensembl; ENST00000424564.2; ENSP00000395041.2; ENSG00000152092.16. [O14525-3]
DR   GeneID; 460; -.
DR   KEGG; hsa:460; -.
DR   MANE-Select; ENST00000361833.7; ENSP00000354536.2; NM_004319.3; NP_004310.1. [O14525-2]
DR   UCSC; uc001glc.5; human. [O14525-1]
DR   CTD; 460; -.
DR   DisGeNET; 460; -.
DR   GeneCards; ASTN1; -.
DR   HGNC; HGNC:773; ASTN1.
DR   HPA; ENSG00000152092; Tissue enhanced (adrenal gland, brain, retina).
DR   MIM; 600904; gene.
DR   neXtProt; NX_O14525; -.
DR   OpenTargets; ENSG00000152092; -.
DR   PharmGKB; PA162376961; -.
DR   VEuPathDB; HostDB:ENSG00000152092; -.
DR   eggNOG; ENOG502R4QT; Eukaryota.
DR   GeneTree; ENSGT00390000003140; -.
DR   HOGENOM; CLU_006316_1_0_1; -.
DR   InParanoid; O14525; -.
DR   OMA; ISMIVRC; -.
DR   OrthoDB; 39300at2759; -.
DR   PhylomeDB; O14525; -.
DR   TreeFam; TF332034; -.
DR   PathwayCommons; O14525; -.
DR   SignaLink; O14525; -.
DR   BioGRID-ORCS; 460; 11 hits in 1071 CRISPR screens.
DR   ChiTaRS; ASTN1; human.
DR   GenomeRNAi; 460; -.
DR   Pharos; O14525; Tbio.
DR   PRO; PR:O14525; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O14525; protein.
DR   Bgee; ENSG00000152092; Expressed in postcentral gyrus and 140 other tissues.
DR   ExpressionAtlas; O14525; baseline and differential.
DR   Genevisible; O14525; HS.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007158; P:neuron cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0001764; P:neuron migration; IBA:GO_Central.
DR   CDD; cd00063; FN3; 1.
DR   InterPro; IPR040685; Annexin-like.
DR   InterPro; IPR045574; ASTN1_2_EGF_Fn.
DR   InterPro; IPR045575; ASTN_1_2_N.
DR   InterPro; IPR026995; Astrotactin.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR020864; MACPF.
DR   PANTHER; PTHR16592; PTHR16592; 1.
DR   Pfam; PF18411; Annexin_like; 1.
DR   Pfam; PF19743; ASTN1_2_EGF_Fn; 1.
DR   Pfam; PF19441; ASTN_1_2_N; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00457; MACPF; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Cytoplasmic vesicle;
KW   Disulfide bond; EGF-like domain; Endosome; Glycoprotein; Membrane;
KW   Methylation; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1302
FT                   /note="Astrotactin-1"
FT                   /id="PRO_0000007481"
FT   TOPO_DOM        22..153
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        384..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        403..1302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:O75129"
FT   DOMAIN          459..507
FT                   /note="EGF-like 1"
FT   DOMAIN          608..652
FT                   /note="EGF-like 2"
FT   DOMAIN          656..708
FT                   /note="EGF-like 3"
FT   DOMAIN          1030..1145
FT                   /note="Fibronectin type-III"
FT   REGION          340..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61137"
FT   MOD_RES         337
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61137"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        729
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        742
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        804
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        984
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        463..475
FT                   /evidence="ECO:0000250"
FT   DISULFID        471..490
FT                   /evidence="ECO:0000250"
FT   DISULFID        492..506
FT                   /evidence="ECO:0000250"
FT   DISULFID        612..625
FT                   /evidence="ECO:0000250"
FT   DISULFID        619..636
FT                   /evidence="ECO:0000250"
FT   DISULFID        638..651
FT                   /evidence="ECO:0000250"
FT   DISULFID        660..672
FT                   /evidence="ECO:0000250"
FT   DISULFID        668..692
FT                   /evidence="ECO:0000250"
FT   DISULFID        694..707
FT                   /evidence="ECO:0000250"
FT   DISULFID        785..951
FT                   /evidence="ECO:0000250|UniProtKB:O75129"
FT   DISULFID        876..941
FT                   /evidence="ECO:0000250|UniProtKB:O75129"
FT   DISULFID        947..954
FT                   /evidence="ECO:0000250|UniProtKB:O75129"
FT   DISULFID        1000..1011
FT                   /evidence="ECO:0000250|UniProtKB:O75129"
FT   DISULFID        1013..1026
FT                   /evidence="ECO:0000250|UniProtKB:O75129"
FT   DISULFID        1101..1121
FT                   /evidence="ECO:0000250|UniProtKB:O75129"
FT   DISULFID        1153..1240
FT                   /evidence="ECO:0000250|UniProtKB:O75129"
FT   DISULFID        1261..1284
FT                   /evidence="ECO:0000250|UniProtKB:O75129"
FT   VAR_SEQ         480..487
FT                   /note="Missing (in isoform 1 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9179496"
FT                   /id="VSP_001371"
FT   VAR_SEQ         1225..1302
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045069"
FT   VARIANT         932
FT                   /note="H -> R (in dbSNP:rs2228956)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9179496"
FT                   /id="VAR_069030"
FT   VARIANT         942
FT                   /note="H -> Q (in dbSNP:rs2281180)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9179496"
FT                   /id="VAR_069031"
FT   VARIANT         1270
FT                   /note="G -> R (in dbSNP:rs12118933)"
FT                   /id="VAR_036764"
FT   VARIANT         1278
FT                   /note="R -> G (in dbSNP:rs12118933)"
FT                   /id="VAR_055713"
FT   CONFLICT        439
FT                   /note="D -> E (in Ref. 2; BAG58151)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        994
FT                   /note="T -> I (in Ref. 2; BAG58151)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        O14525-3:1216
FT                   /note="R -> RYQ (in Ref. 2; BAG58151)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1302 AA;  144913 MW;  CA9EDDA6621C4F3B CRC64;
     MALAGLCALL ACCWGPAAVL ATAAGDVDPS KELECKLKSI TVSALPFLRE NDLSIMHSPS
     ASEPKLLFSV RNDFPGEMVV VDDLENTELP YFVLEISGNT EDIPLVRWRQ QWLENGTLLF
     HIHHQDGAPS LPGQDPTEEP QHESAEEELR ILHISVMGGM IALLLSILCL VMILYTRRRW
     CKRRRVPQPQ KSASAEAANE IHYIPSVLIG GHGRESLRNA RVQGHNSSGT LSIRETPILD
     GYEYDITDLR HHLQRECMNG GEDFASQVTR TLDSLQGCNE KSGMDLTPGS DNAKLSLMNK
     YKDNIIATSP VDSNHQQATL LSHTSSSQRK RINNKARAGS AFLNPEGDSG TEAENDPQLT
     FYTDPSRSRR RSRVGSPRSP VNKTTLTLIS ITSCVIGLVC SSHVNCPLVV KITLHVPEHL
     IADGSRFILL EGSQLDASDW LNPAQVVLFS QQNSSGPWAM DLCARRLLDP CEHQCDPETG
     RREHRAAGEC LCYEGYMKDP VHKHLCIRNE WGTNQGPWPY TIFQRGFDLV LGEQPSDKIF
     RFTYTLGEGM WLPLSKSFVI PPAELAINPS AKCKTDMTVM EDAVEVREEL MTSSSFDSLE
     VLLDSFGPVR DCSKDNGGCS KNFRCISDRK LDSTGCVCPS GLSPMKDSSG CYDRHIGVDC
     SDGFNGGCEQ LCLQQMAPFP DDPTLYNILM FCGCIEDYKL GVDGRSCQLI TETCPEGSDC
     GESRELPMNQ TLFGEMFFGY NNHSKEVAAG QVLKGTFRQN NFARGLDQQL PDGLVVATVP
     LENQCLEEIS EPTPDPDFLT GMVNFSEVSG YPVLQHWKVR SVMYHIKLNQ VAISQALSNA
     LHSLDGATSR ADFVALLDQF GNHYIQEAIY GFEESCSIWY PNKQVQRRLW LEYEDISKGN
     SPSDESEERE RDPKVLTFPE YITSLSDSGT KHMAAGVRME CHSKGRCPSS CPLCHVTSSP
     DTPAEPVLLE VTKAAPIYEL VTNNQTQRLL QEATMSSLWC SGTGDVIEDW CRCDSTAFGA
     DGLPTCAPLP QPVLRLSTVH EPSSTLVVLE WEHSEPPIGV QIVDYLLRQE KVTDRMDHSK
     VETETVLSFV DDIISGAKSP CAMPSQVPDK QLTTISLIIR CLEPDTIYMF TLWGVDNTGR
     RSRPSDVIVK TPCPVVDDVK AQEIADKIYN LFNGYTSGKE QQTAYNTLLD LGSPTLHRVL
     YHYNQHYESF GEFTWRCEDE LGPRKAGLIL SQLGDLSSWC NGLLQEPKIS LRRSSLKYLG
     CRYSEIKPYG LDWAELSRDL RKTCEEQTLS IPYNDYGDSK EI
 
 
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