TMM8B_BOVIN
ID TMM8B_BOVIN Reviewed; 472 AA.
AC A6QLK4; A6QQL1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Transmembrane protein 8B;
DE AltName: Full=Protein NGX6;
GN Name=TMEM8B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia, and Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as a regulator of the EGFR pathway. Probable
CC tumor suppressor which may function in cell growth, proliferation and
CC adhesion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: May interact with EZR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A6NDV4};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:A6NDV4}. Cytoplasm
CC {ECO:0000250|UniProtKB:A6NDV4}. Nucleus {ECO:0000250|UniProtKB:A6NDV4}.
CC Mitochondrion {ECO:0000250|UniProtKB:A6NDV4}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:A6NDV4}. Note=Also detected in mitochondrion and
CC endoplasmic reticulum. {ECO:0000250|UniProtKB:A6NDV4}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TMEM8 family. {ECO:0000305}.
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DR EMBL; BC147996; AAI47997.1; -; mRNA.
DR EMBL; BC149881; AAI49882.1; -; mRNA.
DR RefSeq; NP_001096805.1; NM_001103335.1.
DR AlphaFoldDB; A6QLK4; -.
DR STRING; 9913.ENSBTAP00000015212; -.
DR PaxDb; A6QLK4; -.
DR PRIDE; A6QLK4; -.
DR GeneID; 100125302; -.
DR KEGG; bta:100125302; -.
DR CTD; 51754; -.
DR eggNOG; ENOG502QQ7Q; Eukaryota.
DR HOGENOM; CLU_012979_1_0_1; -.
DR InParanoid; A6QLK4; -.
DR OrthoDB; 704708at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR021910; NGX6/PGAP6/MYMK.
DR PANTHER; PTHR14319; PTHR14319; 1.
DR Pfam; PF12036; DUF3522; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Cytoplasm; Disulfide bond; EGF-like domain;
KW Endoplasmic reticulum; Glycoprotein; Growth regulation; Membrane;
KW Mitochondrion; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..472
FT /note="Transmembrane protein 8B"
FT /id="PRO_0000333038"
FT TOPO_DOM 1..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 182..221
FT /note="EGF-like"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 186..196
FT /evidence="ECO:0000250"
FT DISULFID 190..209
FT /evidence="ECO:0000250"
FT DISULFID 211..220
FT /evidence="ECO:0000250"
SQ SEQUENCE 472 AA; 52088 MW; F38114D6D8B9DFE2 CRC64;
MNMPQSLGNQ PLPPEPPSLR TPAEGPGATS PPEHCWPVRP TLRNELDTFS VHFYIFFGPS
VALPPERPAV FALRLLPVLD SGGVLSLELQ LNVSSLRQEN VTVFGCLTHE VPLSLGDAAV
TCSKESLAGF LLTVSAASRV ARLRIPFPQT GTWFLTLRSL CGVGPRFVRC RNATAEVRLR
TFLSPCVDDC GPYGQCKLLR THNYLYAACE CKAGWRGWGC TDSADALTYG FQLLSTLLLC
LSNLMFLPPV VLAIRSRYVL EAAVYTFTMF FSTFYHACDQ PGIVVFCIMD YDVLQFCDFL
GSLMSVWVTV IAMARLQPVV KQVLYLLGAM LLSMALQLDR HGLWNLLGPS LFALGILATA
WTVRSVRRRH CYPPTWRRWL FCLCPGSLIA GSAILLYAFV ETRDNYFYIH SIWHMLIAGS
VGFLLPPRAK TDRRVPSGAR ARGCGYQLCI NEQEELGLVG PGGATVSSIC AS