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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
 
 
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