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SIGL6_HUMAN
ID   SIGL6_HUMAN             Reviewed;         453 AA.
AC   O43699; A8MV71; B2RTS8; C9JBE5; F8WA78; O15388; O43700;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=Sialic acid-binding Ig-like lectin 6;
DE            Short=Siglec-6;
DE   AltName: Full=CD33 antigen-like 1;
DE   AltName: Full=CDw327;
DE   AltName: Full=Obesity-binding protein 1;
DE            Short=OB-BP1;
DE   AltName: CD_antigen=CD327;
DE   Flags: Precursor;
GN   Name=SIGLEC6; Synonyms=CD33L, CD33L1, OBBP1;
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 [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Placenta;
RX   PubMed=9465907; DOI=10.1159/000134676;
RA   Takei Y., Sasaki S., Fujiwara T., Takahashi E., Muto T., Nakamura Y.;
RT   "Molecular cloning of a novel gene similar to myeloid antigen CD33 and its
RT   specific expression in placenta.";
RL   Cytogenet. Cell Genet. 78:295-300(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), AND VARIANT
RP   VAL-57.
RC   TISSUE=Placenta;
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=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
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   NUCLEOTIDE SEQUENCE [MRNA] OF 3-453 (ISOFORM 1), AND INTERACTION WITH LEP.
RC   TISSUE=Erythroleukemia;
RX   PubMed=10428856; DOI=10.1074/jbc.274.32.22729;
RA   Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C.,
RA   Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F.,
RA   Varki A., Kastelein R.A.;
RT   "OB-BP1/Siglec-6. A leptin- and sialic acid-binding protein of the
RT   immunoglobulin superfamily.";
RL   J. Biol. Chem. 274:22729-22738(1999).
RN   [6]
RP   ERRATUM OF PUBMED:10428856.
RA   Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C.,
RA   Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F.,
RA   Varki A., Kastelein R.A.;
RL   J. Biol. Chem. 274:28058-28058(1999).
CC   -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid
CC       dependent binding to cells. Binds to alpha-2,6-linked sialic acid. The
CC       sialic acid recognition site may be masked by cis interactions with
CC       sialic acids on the same cell surface.
CC   -!- SUBUNIT: Interacts with LEP. {ECO:0000269|PubMed:10428856}.
CC   -!- INTERACTION:
CC       O43699; Q14192: FHL2; NbExp=3; IntAct=EBI-2814604, EBI-701903;
CC       O43699; P15884: TCF4; NbExp=3; IntAct=EBI-2814604, EBI-533224;
CC       O43699-3; Q13021: MALL; NbExp=3; IntAct=EBI-12161783, EBI-750078;
CC       O43699-3; P26367: PAX6; NbExp=3; IntAct=EBI-12161783, EBI-747278;
CC       O43699-3; O00206: TLR4; NbExp=2; IntAct=EBI-12161783, EBI-528701;
CC       O43699-3; Q8N720: ZNF655; NbExp=3; IntAct=EBI-12161783, EBI-625509;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Membrane-bound, CD33L1;
CC         IsoId=O43699-1; Sequence=Displayed;
CC       Name=2; Synonyms=Secreted, CD33L2;
CC         IsoId=O43699-2; Sequence=VSP_002553, VSP_002554;
CC       Name=3;
CC         IsoId=O43699-3; Sequence=VSP_035812;
CC       Name=4;
CC         IsoId=O43699-4; Sequence=VSP_035811, VSP_002553, VSP_002554;
CC       Name=5;
CC         IsoId=O43699-5; Sequence=VSP_045387, VSP_045388;
CC       Name=6;
CC         IsoId=O43699-6; Sequence=VSP_046070, VSP_035812;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in placenta (cyto- and
CC       syncytiotrophoblastic cells) and at lower levels in spleen, peripheral
CC       blood leukocytes (predominantly B-cells) and small intestine.
CC   -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC       the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC       involved in modulation of cellular responses. The phosphorylated ITIM
CC       motif can bind the SH2 domain of several SH2-containing phosphatases.
CC   -!- MISCELLANEOUS: [Isoform 2]: Should not be confused with SIGLEC5 which
CC       has been called CD33L2. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC       acid binding Ig-like lectin) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB70702.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH35359.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI40799.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA24983.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA24984.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Siglec-6;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_273";
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DR   EMBL; D86358; BAA24983.1; ALT_INIT; mRNA.
DR   EMBL; D86359; BAA24984.1; ALT_INIT; mRNA.
DR   EMBL; AK300170; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK300182; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC020914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC035359; AAH35359.2; ALT_INIT; mRNA.
DR   EMBL; BC140798; AAI40799.1; ALT_INIT; mRNA.
DR   EMBL; U71382; AAB70702.1; ALT_INIT; mRNA.
DR   CCDS; CCDS12834.3; -. [O43699-1]
DR   CCDS; CCDS12835.3; -. [O43699-3]
DR   CCDS; CCDS12836.3; -. [O43699-2]
DR   CCDS; CCDS54307.1; -. [O43699-6]
DR   CCDS; CCDS54308.1; -. [O43699-5]
DR   CCDS; CCDS59417.1; -. [O43699-4]
DR   RefSeq; NP_001171018.1; NM_001177547.2. [O43699-6]
DR   RefSeq; NP_001171019.1; NM_001177548.2. [O43699-5]
DR   RefSeq; NP_001171020.1; NM_001177549.2. [O43699-4]
DR   RefSeq; NP_001236.4; NM_001245.6. [O43699-1]
DR   RefSeq; NP_942142.3; NM_198845.5. [O43699-3]
DR   RefSeq; NP_942143.3; NM_198846.5. [O43699-2]
DR   AlphaFoldDB; O43699; -.
DR   SMR; O43699; -.
DR   BioGRID; 107384; 7.
DR   IntAct; O43699; 14.
DR   STRING; 9606.ENSP00000401502; -.
DR   GlyGen; O43699; 5 sites.
DR   iPTMnet; O43699; -.
DR   PhosphoSitePlus; O43699; -.
DR   BioMuta; SIGLEC6; -.
DR   MassIVE; O43699; -.
DR   PaxDb; O43699; -.
DR   PeptideAtlas; O43699; -.
DR   PRIDE; O43699; -.
DR   ProteomicsDB; 30448; -.
DR   ProteomicsDB; 49120; -. [O43699-1]
DR   ProteomicsDB; 49121; -. [O43699-2]
DR   ProteomicsDB; 49122; -. [O43699-3]
DR   ProteomicsDB; 49123; -. [O43699-4]
DR   ProteomicsDB; 9453; -.
DR   Antibodypedia; 2300; 385 antibodies from 34 providers.
DR   DNASU; 946; -.
DR   Ensembl; ENST00000343300.8; ENSP00000345907.4; ENSG00000105492.16. [O43699-2]
DR   Ensembl; ENST00000346477.7; ENSP00000344064.4; ENSG00000105492.16. [O43699-3]
DR   Ensembl; ENST00000359982.8; ENSP00000353071.4; ENSG00000105492.16. [O43699-5]
DR   Ensembl; ENST00000391797.3; ENSP00000375674.3; ENSG00000105492.16. [O43699-4]
DR   Ensembl; ENST00000425629.8; ENSP00000401502.2; ENSG00000105492.16. [O43699-1]
DR   Ensembl; ENST00000436458.5; ENSP00000410679.1; ENSG00000105492.16. [O43699-6]
DR   GeneID; 946; -.
DR   KEGG; hsa:946; -.
DR   MANE-Select; ENST00000425629.8; ENSP00000401502.2; NM_001245.7; NP_001236.4.
DR   UCSC; uc002pwy.4; human. [O43699-1]
DR   CTD; 946; -.
DR   DisGeNET; 946; -.
DR   GeneCards; SIGLEC6; -.
DR   HGNC; HGNC:10875; SIGLEC6.
DR   HPA; ENSG00000105492; Tissue enriched (placenta).
DR   MIM; 604405; gene.
DR   neXtProt; NX_O43699; -.
DR   OpenTargets; ENSG00000105492; -.
DR   PharmGKB; PA35776; -.
DR   VEuPathDB; HostDB:ENSG00000105492; -.
DR   eggNOG; ENOG502S41V; Eukaryota.
DR   GeneTree; ENSGT01040000240469; -.
DR   HOGENOM; CLU_024444_6_1_1; -.
DR   InParanoid; O43699; -.
DR   OMA; HYAFLQF; -.
DR   OrthoDB; 416689at2759; -.
DR   PhylomeDB; O43699; -.
DR   TreeFam; TF332441; -.
DR   PathwayCommons; O43699; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   SignaLink; O43699; -.
DR   BioGRID-ORCS; 946; 13 hits in 1069 CRISPR screens.
DR   ChiTaRS; SIGLEC6; human.
DR   GenomeRNAi; 946; -.
DR   Pharos; O43699; Tbio.
DR   PRO; PR:O43699; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O43699; protein.
DR   Bgee; ENSG00000105492; Expressed in buccal mucosa cell and 95 other tissues.
DR   ExpressionAtlas; O43699; baseline and differential.
DR   Genevisible; O43699; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR013151; Immunoglobulin.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Lectin; Membrane; Reference proteome;
KW   Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..453
FT                   /note="Sialic acid-binding Ig-like lectin 6"
FT                   /id="PRO_0000014946"
FT   TOPO_DOM        27..347
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        369..453
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..123
FT                   /note="Ig-like V-type"
FT   DOMAIN          148..231
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          238..333
FT                   /note="Ig-like C2-type 2"
FT   MOTIF           424..429
FT                   /note="ITIM motif"
FT   MOTIF           444..449
FT                   /note="SLAM-like motif"
FT   BINDING         122
FT                   /ligand="N-acetylneuraminate"
FT                   /ligand_id="ChEBI:CHEBI:35418"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        51..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        166..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        274..319
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         23..58
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046070"
FT   VAR_SEQ         143..153
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035811"
FT   VAR_SEQ         236..252
FT                   /note="YAPQKVAISIFQGNSAA -> S (in isoform 3 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035812"
FT   VAR_SEQ         236
FT                   /note="Y -> WMLRRPPLSTPD (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045387"
FT   VAR_SEQ         339..391
FT                   /note="KPEGRAGGVLGAVWGASITTLVFLCVCFIFRVKTRRKKAAQPVQNTDDVNPV
FT                   M -> SSAPVPDRHSFRPPC (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9465907"
FT                   /id="VSP_002553"
FT   VAR_SEQ         371..453
FT                   /note="KTRRKKAAQPVQNTDDVNPVMVSGSRGHQHQFQTGIVSDHPAEAGPISEDEQ
FT                   ELHYAVLHFHKVQPQEPKVTDTEYSEIKIHK -> ISTSSRQA (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045388"
FT   VAR_SEQ         392..453
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9465907"
FT                   /id="VSP_002554"
FT   VARIANT         57
FT                   /note="L -> V (in dbSNP:rs2305773)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_014252"
FT   VARIANT         262
FT                   /note="L -> F (in dbSNP:rs2005199)"
FT                   /id="VAR_014253"
FT   CONFLICT        6
FT                   /note="E -> K (in Ref. 1; BAA24983/BAA24984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137..138
FT                   /note="LS -> IY (in Ref. 5; AAB70702)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155..161
FT                   /note="TLESGHP -> PGVWPS (in Ref. 5; AAB70702)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="M -> T (in Ref. 2; AK300170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188..189
FT                   /note="TS -> HL (in Ref. 5; AAB70702)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205..206
FT                   /note="RP -> A (in Ref. 5; AAB70702)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        389
FT                   /note="P -> L (in Ref. 2; AK300170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        O43699-5:246
FT                   /note="P -> S (in Ref. 5; AK300182)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   453 AA;  49913 MW;  9DD7FBD8F059E452 CRC64;
     MQGAQEASAS EMLPLLLPLL WAGALAQERR FQLEGPESLT VQEGLCVLVP CRLPTTLPAS
     YYGYGYWFLE GADVPVATND PDEEVQEETR GRFHLLWDPR RKNCSLSIRD ARRRDNAAYF
     FRLKSKWMKY GYTSSKLSVR VMALTHRPNI SIPGTLESGH PSNLTCSVPW VCEQGTPPIF
     SWMSAAPTSL GPRTTQSSVL TITPRPQDHS TNLTCQVTFP GAGVTMERTI QLNVSYAPQK
     VAISIFQGNS AAFKILQNTS SLPVLEGQAL RLLCDADGNP PAHLSWFQGF PALNATPISN
     TGVLELPQVG SAEEGDFTCR AQHPLGSLQI SLSLFVHWKP EGRAGGVLGA VWGASITTLV
     FLCVCFIFRV KTRRKKAAQP VQNTDDVNPV MVSGSRGHQH QFQTGIVSDH PAEAGPISED
     EQELHYAVLH FHKVQPQEPK VTDTEYSEIK IHK
 
 
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