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C209B_MOUSE
ID   C209B_MOUSE             Reviewed;         325 AA.
AC   Q8CJ91; Q8BGZ0; Q8BHK7; Q8CJ86; Q8CJ87; Q8CJ88; Q8CJ89; Q8CJ90; Q8CJ92;
AC   Q8CJ93; Q8CJ94; Q91ZW4; Q91ZX0; Q9D8V4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=CD209 antigen-like protein B;
DE   AltName: Full=DC-SIGN-related protein 1;
DE            Short=DC-SIGNR1;
DE   AltName: Full=OtB7;
DE   AltName: CD_antigen=CD209;
GN   Name=Cd209b;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=11581173; DOI=10.1093/intimm/13.10.1283;
RA   Park C.G., Takahara K., Umemoto E., Yashima Y., Matsubara K., Matsuda Y.,
RA   Clausen B.E., Inaba K., Steinman R.M.;
RT   "Five mouse homologues of the human dendritic cell C-type lectin, DC-
RT   SIGN.";
RL   Int. Immunol. 13:1283-1290(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Swiss Webster; TISSUE=Skin, and Spleen;
RX   PubMed=12137941; DOI=10.1016/s0378-1119(02)00722-9;
RA   Parent S.A., Zhang T., Chrebet G., Clemas J.A., Figueroa D.J., Ky B.,
RA   Blevins R.A., Austin C.P., Rosen H.;
RT   "Molecular characterization of the murine SIGNR1 gene encoding a C-type
RT   lectin homologous to human DC-SIGN and DC-SIGNR.";
RL   Gene 293:33-46(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/cJ; TISSUE=Lymph node;
RX   PubMed=12351402; DOI=10.1182/blood-2002-04-1044;
RA   Geijtenbeek T.B.H., Groot P.C., Nolte M.A., Van Vliet S.J.,
RA   Gangaram-Panday S.T., Van Duijnhoven G.C.F., Kraal G.,
RA   Van Oosterhout A.J.M., Van Kooyk Y.;
RT   "Marginal zone macrophages express a murine homologue of DC-SIGN that
RT   captures blood-borne antigens in vivo.";
RL   Blood 100:2908-2916(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-325 (ISOFORM 1), AND INTERACTION WITH
RP   HIV-1; HIV-2; SIV AND ICAM3.
RX   PubMed=11581396; DOI=10.1128/jvi.75.21.10281-10289.2001;
RA   Baribaud F., Pohlmann S., Sparwasser T., Kimata M.T., Choi Y.K.,
RA   Haggarty B.S., Ahmad N., Macfarlan T., Edwards T.G., Leslie G.J.,
RA   Arnason J., Reinhart T.A., Kimata J.T., Littman D.R., Hoxie J.A.,
RA   Doms R.W.;
RT   "Functional and antigenic characterization of human, rhesus macaque,
RT   pigtailed macaque, and murine DC-SIGN.";
RL   J. Virol. 75:10281-10289(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-325 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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: Probable pathogen-recognition receptor. May mediate the
CC       endocytosis of pathogens which are subsequently degraded in lysosomal
CC       compartments. May recognize in a calcium-dependent manner high mannose
CC       N-linked oligosaccharides in a variety of pathogen antigens. Is a
CC       receptor for ICAM3, probably by binding to mannose-like carbohydrates.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=alpha;
CC         IsoId=Q8CJ91-1; Sequence=Displayed;
CC       Name=2; Synonyms=beta, TM-less;
CC         IsoId=Q8CJ91-2; Sequence=VSP_010069;
CC       Name=3; Synonyms=gamma;
CC         IsoId=Q8CJ91-3; Sequence=VSP_010069, VSP_010070;
CC       Name=4;
CC         IsoId=Q8CJ91-4; Sequence=VSP_010068;
CC   -!- TISSUE SPECIFICITY: Expressed in skin, spleen and lung, probably in a
CC       subset of dendritic cells. Detected in spleen extrafollicular
CC       paracortical areas including the red pulp and marginal zones, and at
CC       lower levels, in the follicular area. Detected in skin suprabasal areas
CC       adjacent to the epidermis and in epidermal cell layer.
CC       {ECO:0000269|PubMed:12137941}.
CC   -!- MISCELLANEOUS: In vitro, is a receptor for HIV-1, HIV-2 and SIV, but
CC       does not transmit virus to permissive T-cells under the conditions
CC       tested.
CC   -!- CAUTION: In mouse, 5 genes homologous to human CD209/DC-SIGN and
CC       CD209L/DC-SIGNR have been identified. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB25166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=SIGNR1;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_00131";
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DR   EMBL; AF373409; AAL13235.1; -; mRNA.
DR   EMBL; AF374471; AAL27540.1; -; mRNA.
DR   EMBL; AF424790; AAN75585.1; -; mRNA.
DR   EMBL; AF424791; AAN75586.1; -; mRNA.
DR   EMBL; AF424792; AAN75587.1; -; mRNA.
DR   EMBL; AF424793; AAN75588.1; -; mRNA.
DR   EMBL; AF424794; AAN75589.1; -; mRNA.
DR   EMBL; AF424795; AAN75590.1; -; mRNA.
DR   EMBL; AF424797; AAN75592.1; -; mRNA.
DR   EMBL; AF424798; AAN75593.1; -; mRNA.
DR   EMBL; AF424796; AAN75591.1; -; mRNA.
DR   EMBL; AF424799; AAN75594.1; -; mRNA.
DR   EMBL; AF424800; AAN75595.1; -; mRNA.
DR   EMBL; AF424801; AAN75596.1; -; mRNA.
DR   EMBL; AF424802; AAN75597.1; -; mRNA.
DR   EMBL; AF422108; AAN31450.1; -; mRNA.
DR   EMBL; AK007656; BAB25166.1; ALT_INIT; mRNA.
DR   CCDS; CCDS22076.1; -. [Q8CJ91-2]
DR   CCDS; CCDS22077.1; -. [Q8CJ91-1]
DR   CCDS; CCDS72089.1; -. [Q8CJ91-3]
DR   RefSeq; NP_001032889.3; NM_001037800.3. [Q8CJ91-2]
DR   RefSeq; NP_001274140.1; NM_001287211.1. [Q8CJ91-3]
DR   RefSeq; NP_081248.4; NM_026972.5. [Q8CJ91-1]
DR   PDB; 3ZHG; X-ray; 1.87 A; A/B/C=191-325, D=190-325.
DR   PDB; 4C9F; X-ray; 2.60 A; A/B/C/D=191-323.
DR   PDB; 4CAJ; X-ray; 2.19 A; A/B/C/D=191-325.
DR   PDBsum; 3ZHG; -.
DR   PDBsum; 4C9F; -.
DR   PDBsum; 4CAJ; -.
DR   AlphaFoldDB; Q8CJ91; -.
DR   SMR; Q8CJ91; -.
DR   DIP; DIP-61328N; -.
DR   STRING; 10090.ENSMUSP00000081104; -.
DR   UniLectin; Q8CJ91; -.
DR   GlyGen; Q8CJ91; 3 sites.
DR   PhosphoSitePlus; Q8CJ91; -.
DR   MaxQB; Q8CJ91; -.
DR   PaxDb; Q8CJ91; -.
DR   PRIDE; Q8CJ91; -.
DR   ProteomicsDB; 265263; -. [Q8CJ91-1]
DR   ProteomicsDB; 265264; -. [Q8CJ91-2]
DR   ProteomicsDB; 265265; -. [Q8CJ91-3]
DR   ProteomicsDB; 265266; -. [Q8CJ91-4]
DR   ABCD; Q8CJ91; 6 sequenced antibodies.
DR   DNASU; 69165; -.
DR   Ensembl; ENSMUST00000084086; ENSMUSP00000081104; ENSMUSG00000065987. [Q8CJ91-1]
DR   Ensembl; ENSMUST00000171635; ENSMUSP00000126070; ENSMUSG00000065987. [Q8CJ91-2]
DR   Ensembl; ENSMUST00000188386; ENSMUSP00000140695; ENSMUSG00000065987. [Q8CJ91-3]
DR   GeneID; 69165; -.
DR   KEGG; mmu:69165; -.
DR   UCSC; uc009ksu.2; mouse. [Q8CJ91-1]
DR   UCSC; uc009ksv.2; mouse. [Q8CJ91-2]
DR   UCSC; uc012fyw.2; mouse. [Q8CJ91-3]
DR   CTD; 69165; -.
DR   MGI; MGI:1916415; Cd209b.
DR   VEuPathDB; HostDB:ENSMUSG00000065987; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000155012; -.
DR   HOGENOM; CLU_049894_7_3_1; -.
DR   InParanoid; Q8CJ91; -.
DR   OMA; VLMNSTC; -.
DR   PhylomeDB; Q8CJ91; -.
DR   TreeFam; TF333341; -.
DR   BioGRID-ORCS; 69165; 2 hits in 73 CRISPR screens.
DR   PRO; PR:Q8CJ91; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8CJ91; protein.
DR   Bgee; ENSMUSG00000065987; Expressed in peripheral lymph node and 43 other tissues.
DR   ExpressionAtlas; Q8CJ91; baseline and differential.
DR   Genevisible; Q8CJ91; MM.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IDA:MGI.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR   GO; GO:0005537; F:mannose binding; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030247; F:polysaccharide binding; IDA:MGI.
DR   GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR   GO; GO:0016045; P:detection of bacterium; IDA:MGI.
DR   GO; GO:0001879; P:detection of yeast; IDA:MGI.
DR   GO; GO:0006897; P:endocytosis; IDA:MGI.
DR   GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
DR   CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR033989; CD209-like_CTLD.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Disulfide bond; Endocytosis;
KW   Glycoprotein; Lectin; Mannose-binding; Membrane; Metal-binding; Receptor;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..325
FT                   /note="CD209 antigen-like protein B"
FT                   /id="PRO_0000046605"
FT   TOPO_DOM        1..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..325
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          201..316
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   BINDING         285
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        195..206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        223..315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        294..307
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   VAR_SEQ         1..183
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12137941"
FT                   /id="VSP_010068"
FT   VAR_SEQ         45..74
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11581173,
FT                   ECO:0000303|PubMed:12137941"
FT                   /id="VSP_010069"
FT   VAR_SEQ         275
FT                   /note="S -> SSRPRHAPISRGRPIYNMHSGR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12137941"
FT                   /id="VSP_010070"
FT   CONFLICT        71
FT                   /note="I -> V (in Ref. 2; AAN75588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="Q -> P (in Ref. 2; AAN75589)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="N -> D (in Ref. 2; AAN75586)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124
FT                   /note="M -> T (in Ref. 2; AAN75585)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="Q -> R (in Ref. 2; AAN75588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="I -> V (in Ref. 2; AAN75586)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="V -> A (in Ref. 2; AAN75588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="Q -> R (in Ref. 2; AAN75589)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="I -> T (in Ref. 2; AAN75587)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="S -> G (in Ref. 2; AAN75587)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        267
FT                   /note="W -> R (in Ref. 2; AAN75589)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="E -> G (in Ref. 2; AAN75585)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="F -> L (in Ref. 2; AAN75597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321..325
FT                   /note="PCTEG -> HA (in Ref. 2; AAN75590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323..325
FT                   /note="TEG -> P (in Ref. 2; AAN75585/AAN75586/AAN75587/
FT                   AAN75588/AAN75589/AAN75591/AAN75592/AAN75593/AAN75594)"
FT                   /evidence="ECO:0000305"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   STRAND          205..209
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   HELIX           216..224
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   TURN            225..227
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   HELIX           236..249
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   STRAND          252..261
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   STRAND          264..267
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   HELIX           275..280
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   TURN            289..291
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   STRAND          301..305
FT                   /evidence="ECO:0007829|PDB:3ZHG"
FT   STRAND          311..318
FT                   /evidence="ECO:0007829|PDB:3ZHG"
SQ   SEQUENCE   325 AA;  37112 MW;  9C9388407C247CA4 CRC64;
     MSDSTEAKMQ PLSSMDDDEL MVSGSRYSIK SSRLRPNSGI KCLAGCSGHS QVPLVLQLLS
     FLFLAGLLLI ILFQVSKTPN TERQKEQEKI LQELTQLTDE LTSRIPISQG KNESMQAKIT
     EQLMQLKTEL LSRIPIFQGQ NESIQEKISE QLMQLKAELL SKISSFPVKD DSKQEKIYQQ
     LVQMKTELFR LCRLCPWDWT FLLGNCYFFS KSQRNWNDAV TACKEVKAQL VIINSDEEQT
     FLQQTSKAKG PTWMGLSDLK KEATWLWVDG STLSSRFQKY WNRGEPNNIG EEDCVEFAGD
     GWNDSKCELK KFWICKKSAT PCTEG
 
 
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