RFTN1_CHICK
ID RFTN1_CHICK Reviewed; 602 AA.
AC Q7SZI5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Raftlin;
DE AltName: Full=Raft-linking protein;
GN Name=RFTN1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12805216; DOI=10.1093/emboj/cdg293;
RA Saeki K., Miura Y., Aki D., Kurosaki T., Yoshimura A.;
RT "The B cell-specific major raft protein, Raftlin, is necessary for the
RT integrity of lipid raft and BCR signal transduction.";
RL EMBO J. 22:3015-3026(2003).
CC -!- FUNCTION: May play a pivotal role in the formation and/or maintenance
CC of lipid rafts. May regulate B-cell antigen receptor-mediated
CC signaling. {ECO:0000269|PubMed:12805216}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Note=Associates with lipid rafts. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the raftlin family. {ECO:0000305}.
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DR EMBL; AB092511; BAC78491.1; -; mRNA.
DR RefSeq; NP_989789.1; NM_204458.1.
DR AlphaFoldDB; Q7SZI5; -.
DR STRING; 9031.ENSGALP00000043108; -.
DR PaxDb; Q7SZI5; -.
DR PRIDE; Q7SZI5; -.
DR GeneID; 395109; -.
DR KEGG; gga:395109; -.
DR CTD; 23180; -.
DR VEuPathDB; HostDB:geneid_395109; -.
DR eggNOG; ENOG502QVP2; Eukaryota.
DR InParanoid; Q7SZI5; -.
DR OrthoDB; 434232at2759; -.
DR PhylomeDB; Q7SZI5; -.
DR PRO; PR:Q7SZI5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR028169; Raftlin.
DR PANTHER; PTHR17601; PTHR17601; 1.
DR Pfam; PF15250; Raftlin; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Lipoprotein; Membrane; Myristate; Palmitate;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..602
FT /note="Raftlin"
FT /id="PRO_0000251955"
FT REGION 178..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 602 AA; 65696 MW; 0D1EF9C453142168 CRC64;
MGCGLNKLEK HDEKRPGNIY STLKRPQVET KIDVSYEYRF LDFTTLNDAE LPGSSAIKLS
SLRDLPAQLQ ELYQQGFVLA AVHPFVQPTD EKEKTPQEQI FRAVLIKKTE RSPKGGIHSE
GYILEVECCS SVNQLSDKKE IPDFIKKIQD AASQGLKFVG IIPQYHSQKN CLVSSSLTPA
SNNSVQSRDN KNVSNCPEDH ASLDGEKIDG INGCSTPAPG EENADQCATS REGRKGEGQA
AEEPDCKSAK GSKEQHEHPG GREAPDTQNG VAENETPARC SKPLTDKTEI FTLFNKPKTP
QRCSQYYTVT IPMRISRNGQ TVNSLEANWL EHMTDHFRKG GSLVNAIFSL GMVNDSLHGT
MDGVFLFEDV AVEDNKTTQG YDAIVVEQWT VLKGVEVQTD YVPLLNSLAI YGWQLTCVLP
TPIVKTNREG NLSTKQIVFL QRPSLPQKAK KKESKFHWRF SKEDMHNKPM KKSRKTKLSS
GEKQTAEKQE FEVTENTRNL AAQLSAASGP GPEQQLDSVI NLGNETAGAD SRGTLHDGVS
EGTCPASADA GDTGGSEVQA CPNQSAPNCC EEQEAAGQDC ALGPDSCQGI DGAAADVEPS
CE