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TR1L1_HUMAN
ID   TR1L1_HUMAN             Reviewed;         369 AA.
AC   Q8N609; Q8N2L7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Translocating chain-associated membrane protein 1-like 1;
GN   Name=TRAM1L1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: Stimulatory or required for the translocation of secretory
CC       proteins across the ER membrane. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8N609; P07307-3: ASGR2; NbExp=3; IntAct=EBI-11996766, EBI-12808270;
CC       Q8N609; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-11996766, EBI-11532900;
CC       Q8N609; P19397: CD53; NbExp=3; IntAct=EBI-11996766, EBI-6657396;
CC       Q8N609; P11912: CD79A; NbExp=3; IntAct=EBI-11996766, EBI-7797864;
CC       Q8N609; Q8TCZ2: CD99L2; NbExp=3; IntAct=EBI-11996766, EBI-2824782;
CC       Q8N609; Q8NC01: CLEC1A; NbExp=3; IntAct=EBI-11996766, EBI-11996768;
CC       Q8N609; Q9BQT9: CLSTN3; NbExp=3; IntAct=EBI-11996766, EBI-11291074;
CC       Q8N609; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-11996766, EBI-6942903;
CC       Q8N609; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-11996766, EBI-2680384;
CC       Q8N609; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-11996766, EBI-781551;
CC       Q8N609; P34910-2: EVI2B; NbExp=3; IntAct=EBI-11996766, EBI-17640610;
CC       Q8N609; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-11996766, EBI-18304435;
CC       Q8N609; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-11996766, EBI-3918971;
CC       Q8N609; Q8TED1: GPX8; NbExp=3; IntAct=EBI-11996766, EBI-11721746;
CC       Q8N609; Q96AG4: LRRC59; NbExp=3; IntAct=EBI-11996766, EBI-358888;
CC       Q8N609; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-11996766, EBI-11956541;
CC       Q8N609; P15941-11: MUC1; NbExp=3; IntAct=EBI-11996766, EBI-17263240;
CC       Q8N609; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-11996766, EBI-742388;
CC       Q8N609; Q53GL0: PLEKHO1; NbExp=3; IntAct=EBI-11996766, EBI-949945;
CC       Q8N609; O43688: PLPP2; NbExp=3; IntAct=EBI-11996766, EBI-722017;
CC       Q8N609; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-11996766, EBI-3920694;
CC       Q8N609; Q6PL24: TMED8; NbExp=5; IntAct=EBI-11996766, EBI-11603430;
CC       Q8N609; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-11996766, EBI-18178701;
CC       Q8N609; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-11996766, EBI-8649725;
CC       Q8N609; Q9Y320: TMX2; NbExp=3; IntAct=EBI-11996766, EBI-6447886;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAM family. {ECO:0000305}.
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DR   EMBL; AK074617; BAC11091.1; -; mRNA.
DR   EMBL; BC030831; AAH30831.1; -; mRNA.
DR   CCDS; CCDS3707.1; -.
DR   RefSeq; NP_689615.2; NM_152402.2.
DR   AlphaFoldDB; Q8N609; -.
DR   BioGRID; 126347; 30.
DR   IntAct; Q8N609; 27.
DR   MINT; Q8N609; -.
DR   STRING; 9606.ENSP00000309402; -.
DR   TCDB; 9.B.311.2.3; the 6-7 tms tram-lag (tram-lag) family.
DR   iPTMnet; Q8N609; -.
DR   PhosphoSitePlus; Q8N609; -.
DR   BioMuta; TRAM1L1; -.
DR   DMDM; 166231532; -.
DR   MassIVE; Q8N609; -.
DR   PaxDb; Q8N609; -.
DR   PeptideAtlas; Q8N609; -.
DR   PRIDE; Q8N609; -.
DR   ProteomicsDB; 72121; -.
DR   Antibodypedia; 26589; 80 antibodies from 16 providers.
DR   DNASU; 133022; -.
DR   Ensembl; ENST00000310754.5; ENSP00000309402.4; ENSG00000174599.5.
DR   GeneID; 133022; -.
DR   KEGG; hsa:133022; -.
DR   MANE-Select; ENST00000310754.5; ENSP00000309402.4; NM_152402.3; NP_689615.2.
DR   UCSC; uc003ibv.5; human.
DR   CTD; 133022; -.
DR   DisGeNET; 133022; -.
DR   GeneCards; TRAM1L1; -.
DR   HGNC; HGNC:28371; TRAM1L1.
DR   HPA; ENSG00000174599; Low tissue specificity.
DR   MIM; 617505; gene.
DR   neXtProt; NX_Q8N609; -.
DR   OpenTargets; ENSG00000174599; -.
DR   PharmGKB; PA134911361; -.
DR   VEuPathDB; HostDB:ENSG00000174599; -.
DR   eggNOG; KOG1608; Eukaryota.
DR   GeneTree; ENSGT00510000046470; -.
DR   HOGENOM; CLU_062830_0_0_1; -.
DR   InParanoid; Q8N609; -.
DR   OMA; SENCLAD; -.
DR   OrthoDB; 831082at2759; -.
DR   PhylomeDB; Q8N609; -.
DR   TreeFam; TF314319; -.
DR   PathwayCommons; Q8N609; -.
DR   SignaLink; Q8N609; -.
DR   BioGRID-ORCS; 133022; 46 hits in 1069 CRISPR screens.
DR   GenomeRNAi; 133022; -.
DR   Pharos; Q8N609; Tdark.
DR   PRO; PR:Q8N609; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q8N609; protein.
DR   Bgee; ENSG00000174599; Expressed in endothelial cell and 162 other tissues.
DR   Genevisible; Q8N609; HS.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0045048; P:protein insertion into ER membrane; IBA:GO_Central.
DR   GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IEA:InterPro.
DR   InterPro; IPR006634; TLC-dom.
DR   InterPro; IPR013599; TRAM1.
DR   InterPro; IPR016447; Translocation_assoc_membrane.
DR   PANTHER; PTHR12371; PTHR12371; 1.
DR   Pfam; PF08390; TRAM1; 1.
DR   Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR   PIRSF; PIRSF005449; Translocation_assoc_membrane; 1.
DR   SMART; SM00724; TLC; 1.
DR   PROSITE; PS50922; TLC; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..369
FT                   /note="Translocating chain-associated membrane protein 1-
FT                   like 1"
FT                   /id="PRO_0000313706"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..81
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..164
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..196
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        216..219
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..297
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          117..326
FT                   /note="TLC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT   REGION          335..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        59
FT                   /note="V -> A (in Ref. 2; AAH30831)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="I -> V (in Ref. 1; BAC11091)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   369 AA;  42162 MW;  95E2A5D82BEECF72 CRC64;
     MGLRKKSTKN PPVLSQEFIL QNHADIVSCV GMFFLLGLVF EGTAEASIVF LTLQHSVAVP
     AAEEQATGSK SLYYYGVKDL ATVFFYMLVA IIIHATIQEY VLDKINKRMQ FTKAKQNKFN
     ESGQFSVFYF FSCIWGTFIL ISENCLSDPT LIWKARPHSM MTFQMKFFYI SQLAYWFHAF
     PELYFQKTKK QDIPRQLVYI GLHLFHITGA YLLYLNHLGL LLLVLHYFVE LLSHMCGLFY
     FSDEKYQKGI SLWAIVFILG RLVTLIVSVL TVGFHLAGSQ NRNPDALTGN VNVLAAKIAV
     LSSSCTIQAY VTWNLITLWL QRWVEDSNIQ ASCMKKKRSR SSKKRTENGV GVETSNRVDC
     PPKRKEKSS
 
 
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