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CD59_MACFA
ID   CD59_MACFA              Reviewed;         128 AA.
AC   Q8SQ46; Q4R5M6; Q8SPI3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=CD59 glycoprotein;
DE   AltName: Full=MAC-inhibitory protein;
DE            Short=MAC-IP;
DE   AltName: Full=Membrane attack complex inhibition factor;
DE            Short=MACIF;
DE   AltName: Full=Protectin;
DE   AltName: CD_antigen=CD59;
DE   Flags: Precursor;
GN   Name=CD59; ORFNames=QccE-13278, QmoA-10351, QnpA-17056;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PHE-72 AND LEU-96.
RC   TISSUE=Medulla oblongata, and Parietal cortex;
RX   PubMed=11991714; DOI=10.1006/geno.2002.6753;
RA   Osada N., Kusuda J., Hirata M., Tanuma R., Hida M., Sugano S., Hirai M.,
RA   Hashimoto K.;
RT   "Search for genes positively selected during primate evolution by 5'-end-
RT   sequence screening of cynomolgus monkey cDNAs.";
RL   Genomics 79:657-662(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Potent inhibitor of the complement membrane attack complex
CC       (MAC) action. Acts by binding to the C8 and/or C9 complements of the
CC       assembling MAC, thereby preventing incorporation of the multiple copies
CC       of C9 required for complete formation of the osmolytic pore (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with T-cell surface antigen CD2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- PTM: N- and O-glycosylated. {ECO:0000250}.
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DR   EMBL; AB072017; BAB86806.1; -; mRNA.
DR   EMBL; AB072018; BAB86807.1; -; mRNA.
DR   EMBL; AB169517; BAE01599.1; -; mRNA.
DR   RefSeq; XP_015289596.1; XM_015434110.1.
DR   AlphaFoldDB; Q8SQ46; -.
DR   SMR; Q8SQ46; -.
DR   STRING; 9541.XP_005578297.1; -.
DR   GeneID; 101867071; -.
DR   CTD; 966; -.
DR   eggNOG; ENOG502SA4P; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IEA:InterPro.
DR   CDD; cd00117; LU; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR018363; CD59_antigen_CS.
DR   InterPro; IPR027101; CD59_glyco.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   PANTHER; PTHR10036:SF9; PTHR10036:SF9; 1.
DR   Pfam; PF00021; UPAR_LY6; 1.
DR   SMART; SM00134; LU; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00983; LY6_UPAR; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..102
FT                   /note="CD59 glycoprotein"
FT                   /id="PRO_0000036110"
FT   PROPEP          103..128
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036111"
FT   DOMAIN          26..108
FT                   /note="UPAR/Ly6"
FT   LIPID           102
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..51
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..38
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..64
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..88
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..94
FT                   /evidence="ECO:0000250"
FT   VARIANT         72
FT                   /note="Y -> F"
FT                   /evidence="ECO:0000269|PubMed:11991714"
FT   VARIANT         96
FT                   /note="F -> L"
FT                   /evidence="ECO:0000269|PubMed:11991714"
SQ   SEQUENCE   128 AA;  14008 MW;  8867D956D63F6E52 CRC64;
     MGIQGGSVLF GLLLVLAVFC HSGHSLQCYN CPNPTTDCKT AINCSSGFDT CLIARAGLQV
     YNQCWKFANC NYNDISTLLK ESELRYFCCK KDLCNFNEQL ESGGTSLSEK TVVLLVTPLL
     AAAWCLHP
 
 
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