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KIF1B_MOUSE
ID   KIF1B_MOUSE             Reviewed;        1816 AA.
AC   Q60575; Q9R0B4; Q9WVE5; Q9Z119;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Kinesin-like protein KIF1B;
GN   Name=Kif1b;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND SUBUNIT.
RC   TISSUE=Brain;
RX   PubMed=7528108; DOI=10.1016/0092-8674(94)90012-4;
RA   Nangaku M., Sato-Yoshitake R., Okada Y., Noda Y., Takemura R., Yamazaki H.,
RA   Hirokawa N.;
RT   "KIF1B, a novel microtubule plus end-directed monomeric motor protein for
RT   transport of mitochondria.";
RL   Cell 79:1209-1220(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=10571041; DOI=10.1016/s0378-1119(99)00370-4;
RA   Gong T.L., Winnicki R.S., Kohrman D.C., Lomax M.I.;
RT   "A novel kinesin of the UNC-104/KIF1 subfamily encoded by the Kif1b gene.";
RL   Gene 239:117-127(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=10341097; DOI=10.1007/s003359901056;
RA   Conforti L., Buckmaster E.A., Tarlton A., Brown M.C., Lyon M.F.,
RA   Perry V.H., Coleman M.P.;
RT   "The major brain isoform of kif1b lacks the putative mitochondria-binding
RT   domain.";
RL   Mamm. Genome 10:617-622(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ICR;
RA   Nakagawa T., Hirokawa N.;
RT   "Identification and characterization of a new kinesin superfamily KIF1B-
RT   beta.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1487, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   INTERACTION WITH MADD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18849981; DOI=10.1038/ncb1785;
RA   Niwa S., Tanaka Y., Hirokawa N.;
RT   "KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator
RT   Rab3 occurs in a GTP-dependent manner through DENN/MADD.";
RL   Nat. Cell Biol. 10:1269-1279(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-647; THR-652; SER-1454 AND
RP   SER-1487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Motor for anterograde transport of mitochondria. Has a
CC       microtubule plus end-directed motility.
CC   -!- FUNCTION: Isoform 1 mediates the transport of synaptic vesicles in
CC       neuronal cells. {ECO:0000250|UniProtKB:O88658}.
CC   -!- SUBUNIT: Monomer (PubMed:7528108). Interacts with KIFBP (By
CC       similarity). Interacts (via C-terminus end of the kinesin-motor domain)
CC       with CHP1; the interaction occurs in a calcium-dependent manner (By
CC       similarity). Interacts with MADD (via death domain) (PubMed:18849981).
CC       {ECO:0000250|UniProtKB:O60333, ECO:0000250|UniProtKB:O88658,
CC       ECO:0000269|PubMed:18849981, ECO:0000269|PubMed:7528108}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Mitochondrion
CC       {ECO:0000250|UniProtKB:O60333}. Cell projection, axon
CC       {ECO:0000269|PubMed:18849981}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory
CC       vesicle, synaptic vesicle {ECO:0000250|UniProtKB:O88658}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q60575-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta;
CC         IsoId=Q60575-2; Sequence=VSP_002862, VSP_002863;
CC       Name=3;
CC         IsoId=Q60575-3; Sequence=VSP_002862, VSP_002863, VSP_002864,
CC                                  VSP_002865;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC       {ECO:0000269|PubMed:18849981}.
CC   -!- DISRUPTION PHENOTYPE: Reduced Rab3 and Madd levels in distal axons of
CC       hippocampal neurons. {ECO:0000269|PubMed:18849981}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; D17577; BAA04503.1; -; mRNA.
DR   EMBL; AF090190; AAF06718.1; -; mRNA.
DR   EMBL; AF131865; AAD39438.1; -; mRNA.
DR   EMBL; AB023656; BAA75243.1; -; mRNA.
DR   CCDS; CCDS18956.1; -. [Q60575-2]
DR   CCDS; CCDS18957.1; -. [Q60575-3]
DR   CCDS; CCDS71521.1; -. [Q60575-1]
DR   PIR; A55289; A55289.
DR   RefSeq; NP_001277924.1; NM_001290995.1. [Q60575-1]
DR   RefSeq; NP_032467.2; NM_008441.2.
DR   AlphaFoldDB; Q60575; -.
DR   SMR; Q60575; -.
DR   BioGRID; 200936; 10.
DR   IntAct; Q60575; 6.
DR   STRING; 10090.ENSMUSP00000061472; -.
DR   iPTMnet; Q60575; -.
DR   PhosphoSitePlus; Q60575; -.
DR   EPD; Q60575; -.
DR   jPOST; Q60575; -.
DR   MaxQB; Q60575; -.
DR   PaxDb; Q60575; -.
DR   PeptideAtlas; Q60575; -.
DR   PRIDE; Q60575; -.
DR   ProteomicsDB; 263600; -. [Q60575-1]
DR   ProteomicsDB; 263601; -. [Q60575-2]
DR   ProteomicsDB; 263602; -. [Q60575-3]
DR   Antibodypedia; 4196; 118 antibodies from 24 providers.
DR   DNASU; 16561; -.
DR   Ensembl; ENSMUST00000055647; ENSMUSP00000061472; ENSMUSG00000063077. [Q60575-2]
DR   Ensembl; ENSMUST00000060537; ENSMUSP00000056754; ENSMUSG00000063077. [Q60575-1]
DR   GeneID; 16561; -.
DR   KEGG; mmu:16561; -.
DR   UCSC; uc008vvy.2; mouse. [Q60575-2]
DR   UCSC; uc008vvz.2; mouse. [Q60575-1]
DR   CTD; 23095; -.
DR   MGI; MGI:108426; Kif1b.
DR   VEuPathDB; HostDB:ENSMUSG00000063077; -.
DR   eggNOG; KOG0245; Eukaryota.
DR   GeneTree; ENSGT00940000157445; -.
DR   HOGENOM; CLU_001485_10_0_1; -.
DR   InParanoid; Q60575; -.
DR   OMA; GSMDQKT; -.
DR   PhylomeDB; Q60575; -.
DR   TreeFam; TF105221; -.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-983189; Kinesins.
DR   BioGRID-ORCS; 16561; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Kif1b; mouse.
DR   PRO; PR:Q60575; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q60575; protein.
DR   Bgee; ENSMUSG00000063077; Expressed in pigmented layer of retina and 271 other tissues.
DR   ExpressionAtlas; Q60575; baseline and differential.
DR   Genevisible; Q60575; MM.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; ISO:MGI.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IMP:UniProtKB.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR   GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR   GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; ISO:MGI.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IDA:UniProtKB.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; NAS:UniProtKB.
DR   GO; GO:0032418; P:lysosome localization; ISO:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; IDA:UniProtKB.
DR   GO; GO:0047497; P:mitochondrion transport along microtubule; IDA:MGI.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
DR   GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:1990778; P:protein localization to cell periphery; ISO:MGI.
DR   GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISO:MGI.
DR   GO; GO:0010970; P:transport along microtubule; ISO:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd00060; FHA; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR24115; PTHR24115; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF49879; SSF49879; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cell projection;
KW   Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Microtubule;
KW   Mitochondrion; Motor protein; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Synapse.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O60333"
FT   CHAIN           2..1816
FT                   /note="Kinesin-like protein KIF1B"
FT                   /id="PRO_0000125408"
FT   DOMAIN          5..354
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   DOMAIN          556..612
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   DOMAIN          1702..1799
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          270..350
FT                   /note="Interaction with KBP"
FT                   /evidence="ECO:0000250"
FT   REGION          1522..1571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1620..1659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          365..386
FT                   /evidence="ECO:0000255"
FT   COILED          470..502
FT                   /evidence="ECO:0000255"
FT   COILED          668..737
FT                   /evidence="ECO:0000255"
FT   COILED          841..869
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1524..1568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60333"
FT   MOD_RES         647
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         652
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1054
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60333"
FT   MOD_RES         1057
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60333"
FT   MOD_RES         1416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60333"
FT   MOD_RES         1454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18630941,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1487
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1573
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60333"
FT   MOD_RES         1603
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60333"
FT   MOD_RES         1610
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60333"
FT   MOD_RES         1613
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60333"
FT   VAR_SEQ         289..294
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:7528108, ECO:0000303|Ref.4"
FT                   /id="VSP_002862"
FT   VAR_SEQ         394..434
FT                   /note="IDPLIDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTA -> T (in
FT                   isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:7528108, ECO:0000303|Ref.4"
FT                   /id="VSP_002863"
FT   VAR_SEQ         707..1196
FT                   /note="YESKLQALQRQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQ
FT                   FTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPVPPELLPSEMEKTHED
FT                   RPFPRTVVAVEVQDLKNGATHYWSLDKLKQRLDLMREMYDRAGEVASSAQDDSETTMTG
FT                   SDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDAMEDFD
FT                   DEAFVDDTGSDAGTEEGSELFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVA
FT                   IVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFSSAAMTR
FT                   SGLSLEELRIVEGQGQSSEVISPPEEVNRMNDLDLKSGTLLDGKMVMEGFSEEIGNHLK
FT                   LGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLGFYHVQN
FT                   IAVEVTESFVDYIKTKPIVFEVFGH -> ADSDSGDDSDKRSCEESWKLITSLREKLPP
FT                   SKLQTIVKKCGLPSSGKKREPIKMYQIPQRRRLSKDSKWVTISDLKIQAVKEICYEVAL
FT                   NDFRHSRQEIEALAIVKMKELCAMYGKKDPNERDSWRAVARDVWDTVGVGDEKIEDMMV
FT                   TGKGGTDVDDLKVHIDKLEDILQEVKKQNNMKDEEIKVLRNKMLKMEKVLPLIGSQEQK
FT                   SQGSHKTKEPLVAGANSVSDNGVSKGESGELGKEERVSQLMNGDPAFRRGRLRWMRQEQ
FT                   IRFKNLQQQEITKQLRRQNVPHRFIPPENRKPRFPFKSNPKHRNSWSPGTHIIITEDEV
FT                   IELRIPKDEEGRKENKEESQEKVGRAASRDVQSAWGTRSQDHIQVSKQHISNQQPPPQL
FT                   RWRSNSLNNGQPKTTRCQATASSESLNSHSGHPTADLQTFQAKRHIHQHRQPYCNYNTG
FT                   GQVEGSTASCCQKQTDKPSHCNQFVTPPRMRRQFSAPNLKAGRETTV (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:7528108"
FT                   /id="VSP_002864"
FT   VAR_SEQ         1197..1816
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:7528108"
FT                   /id="VSP_002865"
FT   CONFLICT        117
FT                   /note="G -> V (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520..523
FT                   /note="GGTL -> RGDI (in Ref. 1; BAA04503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        909
FT                   /note="P -> S (in Ref. 4; BAA75243)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1608..1609
FT                   /note="KL -> TW (in Ref. 3; AAD39438)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1612
FT                   /note="I -> V (in Ref. 3; AAD39438)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1784
FT                   /note="D -> G (in Ref. 4; BAA75243)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1816 AA;  204081 MW;  E316EC295138E5DE CRC64;
     MSGASVKVAV RVRPFNSRET SKESKCIIQM QGNSTSIINP KNPKEAPKSF SFDYSYWSHT
     SPEDPCFASQ NRVYNDIGKE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QEESQAGIIP
     QLCEELFEKI NDNCNEEMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
     LSKLAVTSYT DIADLMDAGN KARTVAATNM NETSSRSHAV FTIVFTQKKQ DPETNLSTEK
     VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVDN CTSKSKKKKK
     TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIKCNAVI
     NEDPNAKLVR ELKEEVTRLK DLLRAQGLGD IIDIDPLIDD YSGSGGKYLK DFQNNKHRYL
     LASENQRPGN FSTASMGSLT SSPSSCSLNS QVGLTSVTSI QERIMSTPGG EEAIERLKES
     EKIIAELNET WEEKLRKTEA IRMEREALLA EMGVAIREDG GTLGVFSPKK TPHLVNLNED
     PLMSECLLYY IKDGITRVGQ ADAERRQDIV LSGAHIKEEH CLFRSERSNT GEVIVTLEPC
     ERSETYVNGK RVAHPVQLRS GNRIIMGKNH VFRFNHPEQA RAEREKTPSA ETPSEPVDWT
     FAQRELLEKQ GIDMKQEMEK RLQEMEILYK KEKEEADLLL EQQRLDYESK LQALQRQVET
     RSLAAETTEE EEEEEEVPWT QHEFELAQWA FRKWKSHQFT SLRDLLWGNA VYLKEANAIS
     VELKKKVQFQ FVLLTDTLYS PVPPELLPSE MEKTHEDRPF PRTVVAVEVQ DLKNGATHYW
     SLDKLKQRLD LMREMYDRAG EVASSAQDDS ETTMTGSDPF YDRFHWFKLV GSSPIFHGCV
     NERLADRTPS PTFSTADSDI TELADEQQDA MEDFDDEAFV DDTGSDAGTE EGSELFSDGH
     DPFYDRSPWF ILVGRAFVYL SNLLYPVPLI HRVAIVSEKG EVRGFLRVAV QAIAADEEAP
     DYGSGIRQSG TAKISFDNEY FNQSDFSSAA MTRSGLSLEE LRIVEGQGQS SEVISPPEEV
     NRMNDLDLKS GTLLDGKMVM EGFSEEIGNH LKLGSAFTFR VTVLQASGIL PEYADIFCQF
     NFLHRHDEAF STEPLKNNGR GSPLGFYHVQ NIAVEVTESF VDYIKTKPIV FEVFGHYQQH
     PLHLQGQDLN SPPQPSRRFF PPPMPLSKPV PATKLNTMNK TTLGQSMSKY DLLVWFEISE
     LEPTGEYIPA VVDHTAGLPC QGTFLLHQGI QRRITVTIIH EKGSELHWKD VRELVVGRIR
     NKPEVDEAAV DAVLSLNIIS AKSLKAAHSS SRTFYRFEAV WDSSLHNSLL LNRVTPYGEK
     IYMTLSAYLE LDHCIQPAVI TKDVCMVFYS RDAKISPPRS LRNLFGSGYS KSPDSNRVTG
     IYELSLCKMA DTGSPGMQRR RRKVLDTSVA YVRGEENLAG WRPRGDSLIL EHQWELEKLE
     LLHEVEKTRH FLLLRERLGD SVPKSLSDSL SPSLSSGTLS TSTSISSQIS TTTFESAITP
     SESSGYDSAD VESLVDREKE LATKCLQLLT HTFNREFSQV HGSISDCKLS DISPIGRDPS
     VSSFSSSTLT PSSTCPSLVD SRSSSMDQKT PEANSRASSP CQEFEQFQIV PTVETPYLAR
     AGKNEFLNLV PDIEEVRAGS VVSKKGYLHF KEPLSSNWAK HFVVVRRPYV FIYNSDKDPV
     ERGIINLSTA QVEYSEDQQA MVKTPNTFAV CTKHRGVLLQ ALNDKDMNDW LYAFNPLLAG
     TIRSKLSRRC PSQPKY
 
 
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