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T106B_RAT
ID   T106B_RAT               Reviewed;         275 AA.
AC   Q6AYA5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Transmembrane protein 106B;
GN   Name=Tmem106b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
RN   [3]
RP   FUNCTION.
RX   PubMed=24357581; DOI=10.1002/embj.201385857;
RA   Schwenk B.M., Lang C.M., Hogl S., Tahirovic S., Orozco D., Rentzsch K.,
RA   Lichtenthaler S.F., Hoogenraad C.C., Capell A., Haass C., Edbauer D.;
RT   "The FTLD risk factor TMEM106B and MAP6 control dendritic trafficking of
RT   lysosomes.";
RL   EMBO J. 33:450-467(2014).
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. {ECO:0000269|PubMed:24357581}.
CC   -!- SUBUNIT: Interacts with MAP6. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q6AYA5; Q63560: Map6; NbExp=6; IntAct=EBI-9316198, EBI-1638469;
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; BC079127; AAH79127.1; -; mRNA.
DR   RefSeq; NP_001004267.1; NM_001004267.1.
DR   AlphaFoldDB; Q6AYA5; -.
DR   BioGRID; 260125; 1.
DR   IntAct; Q6AYA5; 3.
DR   MINT; Q6AYA5; -.
DR   STRING; 10116.ENSRNOP00000008677; -.
DR   GlyGen; Q6AYA5; 5 sites, 7 N-linked glycans (1 site).
DR   iPTMnet; Q6AYA5; -.
DR   PhosphoSitePlus; Q6AYA5; -.
DR   jPOST; Q6AYA5; -.
DR   PaxDb; Q6AYA5; -.
DR   PRIDE; Q6AYA5; -.
DR   DNASU; 312132; -.
DR   Ensembl; ENSRNOT00000008677; ENSRNOP00000008677; ENSRNOG00000006206.
DR   GeneID; 312132; -.
DR   KEGG; rno:312132; -.
DR   UCSC; RGD:1303037; rat.
DR   CTD; 54664; -.
DR   RGD; 1303037; Tmem106b.
DR   eggNOG; ENOG502QQRZ; Eukaryota.
DR   GeneTree; ENSGT00940000158360; -.
DR   HOGENOM; CLU_089337_2_0_1; -.
DR   InParanoid; Q6AYA5; -.
DR   OMA; QTSQERY; -.
DR   OrthoDB; 1175832at2759; -.
DR   PRO; PR:Q6AYA5; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000006206; Expressed in liver and 19 other tissues.
DR   ExpressionAtlas; Q6AYA5; baseline and differential.
DR   Genevisible; Q6AYA5; RN.
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; ISO:RGD.
DR   GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007042; P:lysosomal lumen acidification; ISO:RGD.
DR   GO; GO:1905146; P:lysosomal protein catabolic process; ISO:RGD.
DR   GO; GO:0007041; P:lysosomal transport; ISO:RGD.
DR   GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR   GO; GO:0007040; P:lysosome organization; ISO:RGD.
DR   GO; GO:1900006; P:positive regulation of dendrite development; ISO:RGD.
DR   GO; GO:0051345; P:positive regulation of hydrolase activity; ISO:RGD.
DR   GO; GO:1905671; P:regulation of lysosome organization; ISO:RGD.
DR   InterPro; IPR009790; TMEM106.
DR   PANTHER; PTHR28556; PTHR28556; 1.
DR   Pfam; PF07092; DUF1356; 1.
PE   1: Evidence at protein level;
KW   Endosome; Glycoprotein; Lipoprotein; Lysosome; Membrane; Myristate;
KW   Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix; 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_0000242652"
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   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUM4"
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:0007744|PubMed:24090084"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   275 AA;  31152 MW;  327903F97AE30141 CRC64;
     MGKSLSHLPL HSNKEDGYDG VTSTDNMRNG LVSSEVRNED GRSGDVSQFP YVEFTGRDSV
     TCPTCQGTGR IPRGQENQLV ALIPYSDQRL RPRRTKLYVM ASVFVCLLLS GLAVFFLFPR
     SIDVKYIGVK SAYVSYDSQK RMIYLNITNT LNITNNNYYS VEVENITAQV QFSKTVIGKA
     RLSNITNIGP LDMKQIDYTV PTVIAEEMSY MYDFCTLPSI KVHNIVLMMQ VTVTTAYFGH
     SEQISQERYQ YVDCGRNTTY QLAQSEYLNV LQPQQ
 
 
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