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AR13B_MOUSE
ID   AR13B_MOUSE             Reviewed;         427 AA.
AC   Q640N2; G3X9K5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=ADP-ribosylation factor-like protein 13B;
DE   AltName: Full=ADP-ribosylation factor-like protein 2-like 1;
DE            Short=ARL2-like protein 1;
DE   AltName: Full=Protein hennin;
GN   Name=Arl13b; Synonyms=Arl2l1;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17488627; DOI=10.1016/j.devcel.2007.03.004;
RA   Caspary T., Larkins C.E., Anderson K.V.;
RT   "The graded response to Sonic Hedgehog depends on cilia architecture.";
RL   Dev. Cell 12:767-778(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Lung;
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).
RN   [7]
RP   INTERACTION WITH PIFO.
RX   PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA   Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA   Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT   "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL   Dev. Cell 19:66-77(2010).
RN   [8]
RP   SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-8 AND CYS-9, AND MUTAGENESIS OF
RP   8-CYS-CYS-9.
RX   PubMed=20231383; DOI=10.1083/jcb.200908133;
RA   Cevik S., Hori Y., Kaplan O.I., Kida K., Toivenon T., Foley-Fisher C.,
RA   Cottell D., Katada T., Kontani K., Blacque O.E.;
RT   "Joubert syndrome Arl13b functions at ciliary membranes and stabilizes
RT   protein transport in Caenorhabditis elegans.";
RL   J. Cell Biol. 188:953-969(2010).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21539826; DOI=10.1016/j.ydbio.2011.04.019;
RA   Horner V.L., Caspary T.;
RT   "Disrupted dorsal neural tube BMP signaling in the cilia mutant Arl13b hnn
RT   stems from abnormal Shh signaling.";
RL   Dev. Biol. 355:43-54(2011).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21976698; DOI=10.1091/mbc.e10-12-0994;
RA   Larkins C.E., Aviles G.D., East M.P., Kahn R.A., Caspary T.;
RT   "Arl13b regulates ciliogenesis and the dynamic localization of Shh
RT   signaling proteins.";
RL   Mol. Biol. Cell 22:4694-4703(2011).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22554696; DOI=10.1016/j.ydbio.2012.04.011;
RA   Larkins C.E., Long A.B., Caspary T.;
RT   "Defective Nodal and Cerl2 expression in the Arl13b(hnn) mutant node
RT   underlie its heterotaxia.";
RL   Dev. Biol. 367:15-24(2012).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   AND MUTAGENESIS OF VAL-358.
RX   PubMed=23153492; DOI=10.1016/j.devcel.2012.09.019;
RA   Higginbotham H., Eom T.Y., Mariani L.E., Bachleda A., Hirt J.,
RA   Gukassyan V., Cusack C.L., Lai C., Caspary T., Anton E.S.;
RT   "Arl13b in primary cilia regulates the migration and placement of
RT   interneurons in the developing cerebral cortex.";
RL   Dev. Cell 23:925-938(2012).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23014696; DOI=10.1242/dev.082321;
RA   Su C.Y., Bay S.N., Mariani L.E., Hillman M.J., Caspary T.;
RT   "Temporal deletion of Arl13b reveals that a mispatterned neural tube
RT   corrects cell fate over time.";
RL   Development 139:4062-4071(2012).
RN   [14]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24120134; DOI=10.1016/j.cell.2013.08.060;
RA   Paridaen J.T., Wilsch-Brauninger M., Huttner W.B.;
RT   "Asymmetric inheritance of centrosome-associated primary cilium membrane
RT   directs ciliogenesis after cell division.";
RL   Cell 155:333-344(2013).
RN   [15]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=23817546; DOI=10.1038/nn.3451;
RA   Higginbotham H., Guo J., Yokota Y., Umberger N.L., Su C.Y., Li J.,
RA   Verma N., Hirt J., Ghukasyan V., Caspary T., Anton E.S.;
RT   "Arl13b-regulated cilia activities are essential for polarized radial glial
RT   scaffold formation.";
RL   Nat. Neurosci. 16:1000-1007(2013).
RN   [16]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24339792; DOI=10.1371/journal.pgen.1003977;
RA   Cevik S., Sanders A.A., Van Wijk E., Boldt K., Clarke L., van Reeuwijk J.,
RA   Hori Y., Horn N., Hetterschijt L., Wdowicz A., Mullins A., Kida K.,
RA   Kaplan O.I., van Beersum S.E., Man Wu K., Letteboer S.J., Mans D.A.,
RA   Katada T., Kontani K., Ueffing M., Roepman R., Kremer H., Blacque O.E.;
RT   "Active transport and diffusion barriers restrict Joubert syndrome-
RT   associated ARL13B/ARL-13 to an inv-like ciliary membrane subdomain.";
RL   PLoS Genet. 9:E1003977-E1003977(2013).
RN   [17]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25138100; DOI=10.1038/ejhg.2014.156;
RA   Thomas S., Cantagrel V., Mariani L., Serre V., Lee J.E., Elkhartoufi N.,
RA   de Lonlay P., Desguerre I., Munnich A., Boddaert N., Lyonnet S.,
RA   Vekemans M., Lisgo S.N., Caspary T., Gleeson J., Attie-Bitach T.;
RT   "Identification of a novel ARL13B variant in a Joubert syndrome-affected
RT   patient with retinal impairment and obesity.";
RL   Eur. J. Hum. Genet. 23:621-627(2015).
RN   [18]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH EXOC2.
RX   PubMed=26582389; DOI=10.1091/mbc.e15-02-0061;
RA   Seixas C., Choi S.Y., Polgar N., Umberger N.L., East M.P., Zuo X.,
RA   Moreiras H., Ghossoub R., Benmerah A., Kahn R.A., Fogelgren B., Caspary T.,
RA   Lipschutz J.H., Barral D.C.;
RT   "Arl13b and the exocyst interact synergistically in ciliogenesis.";
RL   Mol. Biol. Cell 27:308-320(2016).
CC   -!- FUNCTION: Cilium-specific protein required to control the microtubule-
CC       based, ciliary axoneme structure. May act by maintaining the
CC       association between IFT subcomplexes A and B. Binds GTP but is not able
CC       to hydrolyze it; the GTPase activity remains unclear. Required to
CC       pattern the neural tube. Involved in cerebral cortex development:
CC       required for the initial formation of a polarized radial glial
CC       scaffold, the first step in the construction of the cerebral cortex, by
CC       regulating ciliary signaling (PubMed:23817546). Regulates the migration
CC       and placement of postmitotic interneurons in the developing cerebral
CC       cortex (PubMed:23153492). {ECO:0000269|PubMed:17488627,
CC       ECO:0000269|PubMed:21539826, ECO:0000269|PubMed:21976698,
CC       ECO:0000269|PubMed:22554696, ECO:0000269|PubMed:23014696,
CC       ECO:0000269|PubMed:23153492, ECO:0000269|PubMed:23817546}.
CC   -!- SUBUNIT: Monomer. Interacts with IFT complex B components IFT46 and
CC       IFT74 (By similarity). Interacts with PIFO (By similarity)
CC       (PubMed:20643351). Interacts with EXOC2; regulates ARL13B localization
CC       to the cilium membrane (PubMed:26582389).
CC       {ECO:0000250|UniProtKB:Q3SXY8, ECO:0000269|PubMed:20643351,
CC       ECO:0000269|PubMed:26582389}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC       {ECO:0000269|PubMed:17488627, ECO:0000269|PubMed:20231383,
CC       ECO:0000269|PubMed:21976698, ECO:0000269|PubMed:23153492,
CC       ECO:0000269|PubMed:23817546, ECO:0000269|PubMed:24120134,
CC       ECO:0000269|PubMed:24339792, ECO:0000269|PubMed:26582389}; Lipid-anchor
CC       {ECO:0000269|PubMed:17488627, ECO:0000269|PubMed:20231383,
CC       ECO:0000269|PubMed:21976698, ECO:0000269|PubMed:23153492,
CC       ECO:0000269|PubMed:23817546, ECO:0000269|PubMed:24120134,
CC       ECO:0000269|PubMed:24339792}. Cell projection, cilium
CC       {ECO:0000269|PubMed:25138100}. Note=Associates to the cilium membrane
CC       via palmitoylation. Localizes to proximal ciliary membranes, to an
CC       inversin-like subciliary membrane compartment, excluding the transition
CC       zone.
CC   -!- TISSUE SPECIFICITY: Cilium-specific protein. Expressed in
CC       neuroepithelial cells and developing radial glia of the developing
CC       cerebral cortex: present in both neuroepithelial and radial progenitor
CC       cells. In radial progenitors, found in the apical, cell soma domains of
CC       these cells (at protein level). Expressed in the primary cilia of
CC       postmitotic cortical neurons during embryonic and postnatal
CC       development. {ECO:0000269|PubMed:23153492,
CC       ECO:0000269|PubMed:23817546}.
CC   -!- PTM: Sumoylation is required for PKD2 entry into cilium. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Impaired cilium's ability to convey critical
CC       extracellular signals such as Shh, without destroying cilia and their
CC       downstream pathways. Mice show a constitutive low-level of Shh activity
CC       owing to loss of modulation of Gli2 activator, corresponding to the
CC       specification of progenitors of motoneurons through most of the neural
CC       tube. In contrast to other mouse mutants that disrupt cilia, Gli3
CC       repressor activity is unaffected in mutants (PubMed:17488627). Mutants
CC       show abnormal cilia in which components of Shh signaling are not
CC       regulated properly: Ptch1 and Smo localize to cilia regardless of Shh
CC       stimulation, and there is no Gli enrichment in cilia upon Shh
CC       stimulation (PubMed:21976698). Conditional deletion disrupts
CC       interneuronal placement, but not postmigratory differentiation in the
CC       developing cerebral cortex (PubMed:23153492). Early neuroepithelial-
CC       specific deletion in cortical progenitors induces a reversal of the
CC       apical-basal polarity of radial progenitors and aberrant neuronal
CC       placement (PubMed:23817546). {ECO:0000269|PubMed:17488627,
CC       ECO:0000269|PubMed:21539826, ECO:0000269|PubMed:21976698,
CC       ECO:0000269|PubMed:22554696, ECO:0000269|PubMed:23014696,
CC       ECO:0000269|PubMed:23153492, ECO:0000269|PubMed:23817546}.
CC   -!- MISCELLANEOUS: Used as a ciliary marker because of its specific
CC       localization to microtubule doublets of the ciliary axoneme. Frequently
CC       used to study cilium signaling, since in contrast to most cilia null
CC       mutants, deletion of Arl13b impairs without destroying cilia and their
CC       downstream pathways (PubMed:23817546). {ECO:0000305|PubMed:23817546}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; AC154309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466521; EDK98235.1; -; Genomic_DNA.
DR   EMBL; BC082574; AAH82574.1; -; mRNA.
DR   CCDS; CCDS28261.1; -.
DR   RefSeq; NP_080853.3; NM_026577.4.
DR   AlphaFoldDB; Q640N2; -.
DR   SMR; Q640N2; -.
DR   STRING; 10090.ENSMUSP00000086703; -.
DR   iPTMnet; Q640N2; -.
DR   PhosphoSitePlus; Q640N2; -.
DR   SwissPalm; Q640N2; -.
DR   jPOST; Q640N2; -.
DR   MaxQB; Q640N2; -.
DR   PaxDb; Q640N2; -.
DR   PeptideAtlas; Q640N2; -.
DR   PRIDE; Q640N2; -.
DR   ProteomicsDB; 277270; -.
DR   ABCD; Q640N2; 1 sequenced antibody.
DR   Antibodypedia; 32073; 133 antibodies from 28 providers.
DR   DNASU; 68146; -.
DR   Ensembl; ENSMUST00000089289; ENSMUSP00000086703; ENSMUSG00000022911.
DR   GeneID; 68146; -.
DR   KEGG; mmu:68146; -.
DR   UCSC; uc007zpu.2; mouse.
DR   CTD; 200894; -.
DR   MGI; MGI:1915396; Arl13b.
DR   VEuPathDB; HostDB:ENSMUSG00000022911; -.
DR   eggNOG; KOG0074; Eukaryota.
DR   eggNOG; KOG0076; Eukaryota.
DR   GeneTree; ENSGT00940000156365; -.
DR   HOGENOM; CLU_040729_3_0_1; -.
DR   InParanoid; Q640N2; -.
DR   OMA; RPNGDAQ; -.
DR   OrthoDB; 732329at2759; -.
DR   PhylomeDB; Q640N2; -.
DR   TreeFam; TF105476; -.
DR   Reactome; R-MMU-5624958; ARL13B-mediated ciliary trafficking of INPP5E.
DR   Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR   Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR   Reactome; R-MMU-9646399; Aggrephagy.
DR   BioGRID-ORCS; 68146; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Arl13b; mouse.
DR   PRO; PR:Q640N2; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q640N2; protein.
DR   Bgee; ENSMUSG00000022911; Expressed in spermatid and 217 other tissues.
DR   ExpressionAtlas; Q640N2; baseline and differential.
DR   Genevisible; Q640N2; MM.
DR   GO; GO:0005930; C:axoneme; IDA:CACAO.
DR   GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031514; C:motile cilium; IDA:MGI.
DR   GO; GO:0097730; C:non-motile cilium; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR   GO; GO:0021943; P:formation of radial glial scaffolds; IMP:UniProtKB.
DR   GO; GO:0001947; P:heart looping; IMP:MGI.
DR   GO; GO:0021830; P:interneuron migration from the subpallium to the cortex; IMP:UniProtKB.
DR   GO; GO:0070986; P:left/right axis specification; IMP:MGI.
DR   GO; GO:0021532; P:neural tube patterning; IMP:UniProtKB.
DR   GO; GO:1905515; P:non-motile cilium assembly; IMP:UniProtKB.
DR   GO; GO:0097500; P:receptor localization to non-motile cilium; IBA:GO_Central.
DR   GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
DR   GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Cilium; Coiled coil; Developmental protein;
KW   GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Palmitate;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..427
FT                   /note="ADP-ribosylation factor-like protein 13B"
FT                   /id="PRO_0000251138"
FT   REGION          207..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          194..285
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        207..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..384
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         28..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..75
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   LIPID           8
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:20231383"
FT   LIPID           9
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:20231383"
FT   MUTAGEN         8..9
FT                   /note="CC->SS: Abolishes palmitoylation and localization to
FT                   the cilium membrane."
FT                   /evidence="ECO:0000269|PubMed:20231383"
FT   MUTAGEN         358
FT                   /note="V->A: Abolishes localization to cilium."
FT                   /evidence="ECO:0000269|PubMed:23153492"
FT   CONFLICT        356
FT                   /note="H -> Q (in Ref. 3; AAH82574)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   427 AA;  48144 MW;  AC131D386B999ABB CRC64;
     MFSLMANCCN LFKRWREPVR KVTLVMVGLD NAGKTATAKG IQGEHPEDVA PTVGFSKIDL
     RQGKFQVTIF DLGGGKRIRG IWKNYYAESY GVIFVVDSSD EERMEETKET MSEVLRHPRI
     SGKPILVLAN KQDKEGALGE ADVIECLSLE KLVNEHKCLC QIEPCSAVLG YGKKIDKSIK
     KGLYWLLHII AKDFDALSER IQKDTTEQRA LEEQEKRERA ERVRKLREER EREQTELDGT
     SGLAEIDSGP VLANPFQPIA AVIIENEKKQ EKEKKKQTVE KDSDVGLLEH KVEPEQAAPQ
     SEADCCLQNP DERVVDSYRE ALSQQLDSED EQDQRGSESG ENSKKKTKKL RMKRSHRVEP
     VNTDESTPKS PTPPQPPPPV GWGTPKVTRL PKLEPLGETR HNDFYGKPLP PLAVRQRPNG
     DAQDTIS
 
 
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