MFSD6_PIG
ID MFSD6_PIG Reviewed; 798 AA.
AC A1DWM3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Major facilitator superfamily domain-containing protein 6;
DE AltName: Full=Macrophage MHC class I receptor 2 homolog;
GN Name=MFSD6; Synonyms=MMR2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bone D.B.J., Hammond J.R.;
RT "Identification of the pig ortholog of hUPP1 in PK15 cells.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. MFSD6 family.
CC {ECO:0000305}.
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DR EMBL; EF065517; ABK96919.1; -; mRNA.
DR RefSeq; NP_001090926.1; NM_001097457.1.
DR RefSeq; XP_005672087.1; XM_005672030.2.
DR RefSeq; XP_005672088.1; XM_005672031.2.
DR AlphaFoldDB; A1DWM3; -.
DR STRING; 9823.ENSSSCP00000017005; -.
DR PaxDb; A1DWM3; -.
DR PeptideAtlas; A1DWM3; -.
DR PRIDE; A1DWM3; -.
DR Ensembl; ENSSSCT00005021671; ENSSSCP00005012944; ENSSSCG00005013876.
DR Ensembl; ENSSSCT00045042492; ENSSSCP00045029507; ENSSSCG00045024719.
DR Ensembl; ENSSSCT00070017651; ENSSSCP00070014638; ENSSSCG00070009097.
DR GeneID; 100037960; -.
DR KEGG; ssc:100037960; -.
DR CTD; 54842; -.
DR eggNOG; KOG3762; Eukaryota.
DR HOGENOM; CLU_013133_2_0_1; -.
DR InParanoid; A1DWM3; -.
DR OrthoDB; 628784at2759; -.
DR TreeFam; TF314366; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 15.
DR Genevisible; A1DWM3; SS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 3.
DR InterPro; IPR024989; MFS_assoc_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF12832; MFS_1_like; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 2: Evidence at transcript level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..798
FT /note="Major facilitator superfamily domain-containing
FT protein 6"
FT /id="PRO_0000321942"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 25..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSS7"
SQ SEQUENCE 798 AA; 88389 MW; 5ACEC180ACFFEB30 CRC64;
MATDDKVAIL TDDEEEQKRK YVLADPFNGI SREPEPPSNE TPSPSESAAI PEEETDWIEK
HCVKINNDLL ISKVFYFFFY SAYGSLYPLL PVYYKQLGMS PSQSGLLVGI RYFIEFCSAP
FWGVVADRFK KGKVVLLFSL LCWVLFNLGI GFVKPATLRC VPKIPPTARP TNSSHPFTIL
PANSSIVPSI TTSTRTREKR NLPPYDGLEM LVSEPNVTET VIFSTAPNKT SAPTLQPQTD
EITDRVMDLT SHPSTAPSTP PGNTTRETTT SLVTTTKSLP SDQVTLVYDQ QEVEAIFLVI
LVVVIIGEFF SASSVTIVDT VTLQYLGKHR DRYGLQRMWG SLGWGLAMLS VGIGIDYTHI
DVLIDGKGCK PPEYRNYQIV FIVFGVLMTM ALIVATQFRF RYNHFKNGEN KGKEVEIPQV
ERNSSTECSE ETPTTTSHSQ AFNFWDLIRL LCSVQYGSVL FVAWFMGFGY GFVFTFLYWH
LEDLNGTTTL FGVCSVLSHV SELTAYFFSH KLIELIGHIR VLYIGLACNT ARYIYISYLE
NAWTVLPMEV LQGVTHAAIW AACISYLSAA VPPELRTSAQ GILQGLHLGL GRGCGAMIGG
VLVNYFGAAA TFRGIGMACL VILLLFALIQ WLAVPDEEED KTMLAERIPV PSSPVPIATI
DLVQQQTEDV MPRIEPRLPP KKTKHQEEQE DVNKPAWGVS SSPWVTFVYA LYQIKEMMQL
TRDNRASEIQ PLQGTSENRE SPPAGGGTLP GPCETHSDPS RNQPSPQAAA ASQTQSSPAR
PRVEESEDQQ AQPAAGGH