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LEC_ALOAR
ID   LEC_ALOAR               Reviewed;         109 AA.
AC   P49329;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Mannose-specific lectin;
DE   AltName: Full=Agglutinin;
DE   Contains:
DE     RecName: Full=Mannose-specific lectin heavy chain;
DE   Contains:
DE     RecName: Full=Mannose-specific lectin light chain;
DE   Flags: Precursor;
OS   Aloe arborescens (Kidachi aloe).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asphodelaceae;
OC   Asphodeloideae; Aloe.
OX   NCBI_TaxID=45385;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=cv. Natalensis Berger; TISSUE=Leaf;
RX   PubMed=7669035; DOI=10.1006/bbrc.1995.2270;
RA   Koike T., Titani K., Suzuki M., Beppu H., Kuzuya H., Maruta K., Shimpo K.,
RA   Fujita K.;
RT   "The complete amino acid sequence of a mannose-binding lectin from 'Kidachi
RT   Aloe' (Aloe arborescens Miller var. natalensis Berger).";
RL   Biochem. Biophys. Res. Commun. 214:163-170(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-24 AND 83-106.
RC   STRAIN=cv. Natalensis Berger; TISSUE=Leaf;
RX   PubMed=8720136; DOI=10.1093/oxfordjournals.jbchem.a125008;
RA   Koike T., Beppu H., Kuzuya H., Maruta K., Shimpo K., Suzuki M., Titani K.,
RA   Fujita K.;
RT   "A 35 kDa mannose-binding lectin with hemagglutinating and mitogenic
RT   activities from 'Kidachi Aloe' (Aloe arborescens Miller var. natalensis
RT   Berger).";
RL   J. Biochem. 118:1205-1210(1995).
CC   -!- FUNCTION: Mannose-specific lectin. Shows agglutinating activity toward
CC       rabbit erythrocytes and mitogenic activity towards mouse lymphocytes.
CC   -!- SUBUNIT: Homotrimer or homotetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   AlphaFoldDB; P49329; -.
DR   SMR; P49329; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   CDD; cd00028; B_lectin; 1.
DR   Gene3D; 2.90.10.10; -; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   SMART; SM00108; B_lectin; 1.
DR   SUPFAM; SSF51110; SSF51110; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Lectin; Mannose-binding;
KW   Secreted.
FT   CHAIN           1..78
FT                   /note="Mannose-specific lectin heavy chain"
FT                   /id="PRO_0000021583"
FT   PROPEP          79..82
FT                   /evidence="ECO:0000269|PubMed:8720136"
FT                   /id="PRO_0000021584"
FT   CHAIN           83..109
FT                   /note="Mannose-specific lectin light chain"
FT                   /id="PRO_0000021585"
FT   DOMAIN          1..109
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DISULFID        29..52
FT   VARIANT         63
FT                   /note="V -> I"
FT   VARIANT         76
FT                   /note="N -> F"
FT   VARIANT         94
FT                   /note="N -> D"
FT   VARIANT         104
FT                   /note="A -> S"
SQ   SEQUENCE   109 AA;  11941 MW;  31EB94D2A4274DE9 CRC64;
     DNILYSSEVL HENQYISYGP YEFIMQHDCN LVLYESGNPT WASNTGGLAL HCRATLQTDG
     NLVVQNSANR IIWQSNTGTG TNGDYLLVLQ KNGNVVIVGP PIWATGTGR
 
 
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