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WNT7A_MOUSE
ID   WNT7A_MOUSE             Reviewed;         349 AA.
AC   P24383; Q80VH3; Q9DBY3;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Protein Wnt-7a;
DE   Flags: Precursor;
GN   Name=Wnt7a; Synonyms=Wnt-7a;
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].
RX   PubMed=2279700; DOI=10.1101/gad.4.12b.2319;
RA   Gavin B.J., McMahon J.A., McMahon A.P.;
RT   "Expression of multiple novel Wnt-1/int-1-related genes during fetal and
RT   adult mouse development.";
RL   Genes Dev. 4:2319-2332(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
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   [5]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=7885472; DOI=10.1038/374350a0;
RA   Parr B.A., McMahon A.P.;
RT   "Dorsalizing signal Wnt-7a required for normal polarity of D-V and A-P axes
RT   of mouse limb.";
RL   Nature 374:350-353(1995).
RN   [6]
RP   FUNCTION, AND DISEASE.
RX   PubMed=9769174; DOI=10.1006/dbio.1998.9007;
RA   Parr B.A., Avery E.J., Cygan J.A., McMahon A.P.;
RT   "The classical mouse mutant postaxial hemimelia results from a mutation in
RT   the Wnt 7a gene.";
RL   Dev. Biol. 202:228-234(1998).
RN   [7]
RP   FUNCTION.
RX   PubMed=9790192; DOI=10.1038/27221;
RA   Parr B.A., McMahon A.P.;
RT   "Sexually dimorphic development of the mammalian reproductive tract
RT   requires Wnt-7a.";
RL   Nature 395:707-710(1998).
RN   [8]
RP   INTERACTION WITH PORCN.
RX   PubMed=10866835; DOI=10.1046/j.1432-1033.2000.01478.x;
RA   Tanaka K., Okabayashi H., Asashima M., Perrimon N., Kadowaki T.;
RT   "The evolutionarily conserved porcupine gene family is involved in the
RT   processing of the Wnt family.";
RL   Eur. J. Biochem. 267:4300-4311(2000).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH FZD5.
RX   PubMed=18230341; DOI=10.1016/j.bbrc.2008.01.088;
RA   Carmon K.S., Loose D.S.;
RT   "Wnt7a interaction with Fzd5 and detection of signaling activation using a
RT   split eGFP.";
RL   Biochem. Biophys. Res. Commun. 368:285-291(2008).
RN   [10]
RP   FUNCTION, INTERACTION WITH FZD5, AND SUBCELLULAR LOCATION.
RX   PubMed=20530549; DOI=10.1242/dev.046722;
RA   Sahores M., Gibb A., Salinas P.C.;
RT   "Frizzled-5, a receptor for the synaptic organizer Wnt7a, regulates
RT   activity-mediated synaptogenesis.";
RL   Development 137:2215-2225(2010).
RN   [11]
RP   FUNCTION.
RX   PubMed=23629626; DOI=10.1128/mcb.00325-13;
RA   Qu Q., Sun G., Murai K., Ye P., Li W., Asuelime G., Cheung Y.T., Shi Y.;
RT   "Wnt7a regulates multiple steps of neurogenesis.";
RL   Mol. Cell. Biol. 33:2551-2559(2013).
RN   [12]
RP   FUNCTION.
RX   PubMed=28803732; DOI=10.1016/j.neuron.2017.07.031;
RA   Cho C., Smallwood P.M., Nathans J.;
RT   "Reck and Gpr124 Are Essential Receptor Cofactors for Wnt7a/Wnt7b-specific
RT   signaling in mammalian CNS angiogenesis and blood-brain barrier
RT   regulation.";
RL   Neuron 95:1056-1073(2017).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors that functions in the canonical Wnt/beta-
CC       catenin signaling pathway (PubMed:18230341, PubMed:20530549,
CC       PubMed:23629626). Plays an important role in embryonic development,
CC       including dorsal versus ventral patterning during limb development,
CC       skeleton development and urogenital tract development (PubMed:7885472,
CC       PubMed:9769174, PubMed:9790192). Required for central nervous system
CC       (CNS) angiogenesis and blood-brain barrier regulation
CC       (PubMed:28803732). Required for normal, sexually dimorphic development
CC       of the Mullerian ducts, and for normal fertility in both sexes
CC       (PubMed:9790192). Required for normal neural stem cell proliferation in
CC       the hippocampus dentate gyrus (PubMed:23629626). Required for normal
CC       progress through the cell cycle in neural progenitor cells, for self-
CC       renewal of neural stem cells, and for normal neuronal differentiation
CC       and maturation (PubMed:23629626). Promotes formation of synapses via
CC       its interaction with FZD5 (PubMed:20530549).
CC       {ECO:0000269|PubMed:18230341, ECO:0000269|PubMed:20530549,
CC       ECO:0000269|PubMed:23629626, ECO:0000269|PubMed:28803732,
CC       ECO:0000269|PubMed:7885472, ECO:0000269|PubMed:9769174,
CC       ECO:0000269|PubMed:9790192}.
CC   -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC       oligomerization and is required for prolonged biological activity (By
CC       similarity). The complex with AFM may represent the physiological form
CC       in body fluids (By similarity). Interacts with FZD5 (PubMed:18230341,
CC       PubMed:20530549). Interacts with PORCN (PubMed:10866835). Interacts
CC       (via intrinsically disordered linker region) with RECK; interaction
CC       with RECK confers ligand selectivity for Wnt7 in brain endothelial
CC       cells and allows these cells to selectively respond to Wnt7 (By
CC       similarity). {ECO:0000250|UniProtKB:O00755,
CC       ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:18230341,
CC       ECO:0000269|PubMed:20530549}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000305}. Secreted {ECO:0000305|PubMed:20530549}.
CC   -!- DEVELOPMENTAL STAGE: Detected in the flanking ectoderm of the trunk
CC       prior to limb outgrowth. First detected in the presumptive forelimb
CC       region at 8.75 dpc, and in the presumptive hindlimb region at 9.25 dpc.
CC       Uniformly distributed throughout the dorsal limb ectoderm during the
CC       initial stages of limb-bud outgrowth (9.25 dpc for the forelimbs, 9.75
CC       dpc for the hindlimbs). {ECO:0000269|PubMed:7885472}.
CC   -!- DOMAIN: The intrinsically disordered linker region is required for
CC       recognition by RECK in brain endothelial cells.
CC       {ECO:0000250|UniProtKB:O00755}.
CC   -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC       receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC       inhibition. {ECO:0000250|UniProtKB:P27467,
CC       ECO:0000250|UniProtKB:P56704}.
CC   -!- DISEASE: Note=Defects in Wnt7a cause the postaxial hemimelia (px)
CC       phenotype that is characterized by limb patterning defects accompanied
CC       by Mullerian duct-associated sterility in both sexes.
CC       {ECO:0000269|PubMed:9769174}.
CC   -!- MISCELLANEOUS: Male mice lacking Wnt7a fail to undergo regression of
CC       the Mullerian duct as a result of the absence of the receptor for
CC       Mullerian-inhibiting substance. In males, mature sperm fills the vas
CC       deferens, but sperm exit is blocked due to the persistence of the
CC       Mullerian duct, causing male sterility. Wnt7a deficient females are
CC       infertile because of abnormal development of the oviduct and uterus,
CC       both of which are Mullerian duct derivatives.
CC       {ECO:0000269|PubMed:9790192}.
CC   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR   EMBL; M89801; AAA40570.1; -; mRNA.
DR   EMBL; AK004683; BAB23470.1; -; mRNA.
DR   EMBL; CH466523; EDK99298.1; -; Genomic_DNA.
DR   EMBL; BC049093; AAH49093.2; -; mRNA.
DR   EMBL; BC057586; AAH57586.1; -; mRNA.
DR   CCDS; CCDS39568.1; -.
DR   PIR; G36470; G36470.
DR   RefSeq; NP_033553.2; NM_009527.3.
DR   AlphaFoldDB; P24383; -.
DR   SMR; P24383; -.
DR   BioGRID; 204580; 6.
DR   STRING; 10090.ENSMUSP00000032180; -.
DR   GlyGen; P24383; 3 sites.
DR   PhosphoSitePlus; P24383; -.
DR   PaxDb; P24383; -.
DR   PRIDE; P24383; -.
DR   ProteomicsDB; 297856; -.
DR   Antibodypedia; 2520; 211 antibodies from 30 providers.
DR   DNASU; 22421; -.
DR   Ensembl; ENSMUST00000032180; ENSMUSP00000032180; ENSMUSG00000030093.
DR   GeneID; 22421; -.
DR   KEGG; mmu:22421; -.
DR   UCSC; uc009cxz.1; mouse.
DR   CTD; 7476; -.
DR   MGI; MGI:98961; Wnt7a.
DR   VEuPathDB; HostDB:ENSMUSG00000030093; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000158523; -.
DR   HOGENOM; CLU_033039_1_4_1; -.
DR   InParanoid; P24383; -.
DR   OMA; VQHISGC; -.
DR   OrthoDB; 745245at2759; -.
DR   PhylomeDB; P24383; -.
DR   TreeFam; TF105310; -.
DR   Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR   BioGRID-ORCS; 22421; 3 hits in 74 CRISPR screens.
DR   PRO; PR:P24383; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P24383; protein.
DR   Bgee; ENSMUSG00000030093; Expressed in external ectoderm and 163 other tissues.
DR   Genevisible; P24383; MM.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0005125; F:cytokine activity; ISO:MGI.
DR   GO; GO:0005109; F:frizzled binding; IPI:MGI.
DR   GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IGI:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
DR   GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR   GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IDA:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0001502; P:cartilage condensation; ISO:MGI.
DR   GO; GO:0051216; P:cartilage development; IDA:BHF-UCL.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0021846; P:cell proliferation in forebrain; ISO:MGI.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:MGI.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0022009; P:central nervous system vasculogenesis; IGI:MGI.
DR   GO; GO:0021707; P:cerebellar granule cell differentiation; IDA:MGI.
DR   GO; GO:0002062; P:chondrocyte differentiation; ISO:MGI.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR   GO; GO:0000578; P:embryonic axis specification; ISO:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; ISO:MGI.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IGI:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IGI:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR   GO; GO:0030010; P:establishment of cell polarity; IDA:MGI.
DR   GO; GO:0060173; P:limb development; IDA:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; ISO:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   GO; GO:0035567; P:non-canonical Wnt signaling pathway; IGI:MGI.
DR   GO; GO:0060066; P:oviduct development; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:MGI.
DR   GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISO:MGI.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IGI:ParkinsonsUK-UCL.
DR   GO; GO:1904891; P:positive regulation of excitatory synapse assembly; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0031133; P:regulation of axon diameter; IDA:MGI.
DR   GO; GO:0050770; P:regulation of axonogenesis; IDA:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR   GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IMP:MGI.
DR   GO; GO:0062009; P:secondary palate development; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   GO; GO:0014719; P:skeletal muscle satellite cell activation; IDA:MGI.
DR   GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IDA:MGI.
DR   GO; GO:0048103; P:somatic stem cell division; IDA:MGI.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR   GO; GO:0048864; P:stem cell development; ISO:MGI.
DR   GO; GO:0007416; P:synapse assembly; IDA:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   GO; GO:0060065; P:uterus development; IMP:MGI.
DR   GO; GO:0061038; P:uterus morphogenesis; IMP:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; ISO:MGI.
DR   GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISO:MGI.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR013300; Wnt7.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01891; WNT7PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..349
FT                   /note="Protein Wnt-7a"
FT                   /id="PRO_0000041443"
FT   REGION          238..266
FT                   /note="Disordered linker"
FT                   /evidence="ECO:0000250|UniProtKB:O00755"
FT   LIPID           206
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        73..84
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        123..131
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        133..152
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        200..214
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        202..209
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        278..309
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        294..304
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        308..348
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        324..339
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        326..336
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        331..332
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   CONFLICT        143
FT                   /note="R -> W (in Ref. 1; AAA40570)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="K -> L (in Ref. 1; AAA40570)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   349 AA;  38974 MW;  C36ACDF7930790A1 CRC64;
     MTRKARRCLG HLFLSLGIVY LRIGGFSSVV ALGASIICNK IPGLAPRQRA ICQSRPDAII
     VIGEGSQMGL DECQFQFRNG RWNCSALGER TVFGKELKVG SREAAFTYAI IAAGVAHAIT
     AACTQGNLSD CGCDKEKQGQ YHRDEGWKWG GCSADIRYGI GFAKVFVDAR EIKQNARTLM
     NLHNNEAGRK ILEENMKLEC KCHGVSGSCT TKTCWTTLPQ FRELGYVLKD KYNEAVHVEP
     VRASRNKRPT FLKIKKPLSY RKPMDTDLVY IEKSPNYCEE DPVTGSVGTQ GRACNKTAPQ
     ASGCDLMCCG RGYNTHQYAR VWQCNCKFHW CCYVKCNTCS ERTEMYTCK
 
 
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