T106B_BOVIN
ID T106B_BOVIN Reviewed; 275 AA.
AC Q3ZC25;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Transmembrane protein 106B;
GN Name=TMEM106B;
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=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in dendrite morphogenesis and maintenance by
CC regulating lysosomal trafficking via its interaction with MAP6. May act
CC by inhibiting retrograde transport of lysosomes along dendrites.
CC Required for dendrite branching (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAP6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Single-pass
CC type II membrane protein. Lysosome membrane {ECO:0000250}; Single-pass
CC type II membrane protein. Membrane {ECO:0000250|UniProtKB:Q9NUM4};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q9NUM4}.
CC -!- SIMILARITY: Belongs to the TMEM106 family. {ECO:0000305}.
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DR EMBL; BC102965; AAI02966.1; -; mRNA.
DR RefSeq; NP_001029509.1; NM_001034337.1.
DR RefSeq; XP_015323767.1; XM_015468281.1.
DR RefSeq; XP_015323769.1; XM_015468283.1.
DR AlphaFoldDB; Q3ZC25; -.
DR STRING; 9913.ENSBTAP00000026319; -.
DR PaxDb; Q3ZC25; -.
DR Ensembl; ENSBTAT00000026319; ENSBTAP00000026319; ENSBTAG00000019750.
DR GeneID; 508903; -.
DR KEGG; bta:508903; -.
DR CTD; 54664; -.
DR VEuPathDB; HostDB:ENSBTAG00000019750; -.
DR VGNC; VGNC:35945; TMEM106B.
DR eggNOG; ENOG502QQRZ; Eukaryota.
DR GeneTree; ENSGT00940000158360; -.
DR HOGENOM; CLU_089337_2_0_1; -.
DR InParanoid; Q3ZC25; -.
DR OMA; QTSQERY; -.
DR OrthoDB; 1175832at2759; -.
DR TreeFam; TF328907; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000019750; Expressed in occipital lobe and 109 other tissues.
DR ExpressionAtlas; Q3ZC25; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0007041; P:lysosomal transport; IBA:GO_Central.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR InterPro; IPR009790; TMEM106.
DR PANTHER; PTHR28556; PTHR28556; 1.
DR Pfam; PF07092; DUF1356; 1.
PE 2: Evidence at transcript level;
KW Endosome; Glycoprotein; Lipoprotein; Lysosome; Membrane; Myristate;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NUM4"
FT CHAIN 2..275
FT /note="Transmembrane protein 106B"
FT /id="PRO_0000242649"
FT TOPO_DOM 2..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..275
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUM4"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 275 AA; 31213 MW; 33EE73967C885A43 CRC64;
MGKSFSHLPL HSNKEDGYDG MTSTENIRNG LVNGEVHNED GRSGDVSQFP YVEFTGRDSV
TCPTCQGTGR IPRGQENQLV ALIPYSDQRL RPRRTKLYVM ASVFVCLLLS GLAVFFLFPR
SIDVKYIGVK SAYVSYDVQK RTIYLNITNT LNITNNNYYS VEVENITAQV QFSKTVIGKA
RLNNITSIGP LDMKQIDYTV PTVIAEEMSY MFDFCTLLTI KVHNIVLMMQ VTVTTTYFGH
SEQISQERYQ YVDCGRNTTY HLGQSEYLNV LQPQQ