RFTN2_PONAB
ID RFTN2_PONAB Reviewed; 501 AA.
AC Q5R458;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Raftlin-2;
DE AltName: Full=Raft-linking protein 2;
GN Name=RFTN2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Upon bacterial lipopolysaccharide stimulation, mediates
CC clathrin-dependent internalization of TLR4 in dendritic cells,
CC resulting in activation of TICAM1-mediated signaling and subsequent
CC IFNB1 production. May regulate B-cell antigen receptor mediated-
CC signaling. {ECO:0000250|UniProtKB:Q8CHX7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14699};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q14699}.
CC -!- SIMILARITY: Belongs to the raftlin family. {ECO:0000305}.
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DR EMBL; CR861400; CAH93458.1; -; mRNA.
DR RefSeq; NP_001127026.1; NM_001133554.1.
DR AlphaFoldDB; Q5R458; -.
DR STRING; 9601.ENSPPYP00000014580; -.
DR GeneID; 100174051; -.
DR KEGG; pon:100174051; -.
DR CTD; 130132; -.
DR eggNOG; ENOG502QVRY; Eukaryota.
DR InParanoid; Q5R458; -.
DR OrthoDB; 434232at2759; -.
DR Proteomes; UP000001595; 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; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..501
FT /note="Raftlin-2"
FT /id="PRO_0000089340"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHX7"
FT MOD_RES 409
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHX7"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHX7"
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 501 AA; 55940 MW; 70D3CF43852DB548 CRC64;
MGCGLRKLED PDDSSPGKIF STLKRPQVET KTEFAYEYVL LDFTLQASSN PEVIKINSIL
DIVTKVEDYY LKGYIVGAIH PVIQPVGQRK HLPASCLYRV VLSRLKLSPK NSAAPSGQRR
PRLVIEECPL TSEAQTNDAA KELIEKINFA AKRGMKFVGF ISQPYSPYKF CNGTNHDGDI
ESMLHVRHSS DENCRSWNEG TLSGQSSESG IEEELHHESG QYPMEQNGSP SSSKSRKGEA
SDNKLYTVFN AFDDDSTSWT YQEGILSMKV TRKGSVISTL DADWLELTTF YYKQGLSLID
SFVFWETSKG EHLPKSLEGF FIYEEEGSGV PGSSRKGNDA IVVEQWTVIE GCEIKTDYGP
LLHTLAEFGW LLTSVLPTPV LRHDSEGNLA TKQIVFLQRP VMWNSAAQTT DKKASRRIKG
EDKNKATSRS IGLDTTTPQP AESRHPPEEC RLSPSRECWT KEGRLAQHNS FSGFSSSDSV
LRELDDGQFD QEDGVTQVTC M