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TM9S1_MOUSE
ID   TM9S1_MOUSE             Reviewed;         606 AA.
AC   Q9DBU0; Q3U7S4; Q8VD27; Q922J5; Q9ET29;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Transmembrane 9 superfamily member 1;
DE   Flags: Precursor;
GN   Name=Tm9sf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Warner S.J., Lomax M.I.;
RT   "Evolution of the TM9 super family of membrane spanning proteins.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
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: Plays an essential role in autophagy. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein.
CC       Cytoplasmic vesicle, autophagosome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
CC       {ECO:0000305}.
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DR   EMBL; AF269152; AAF98161.1; -; mRNA.
DR   EMBL; AK004754; BAB23535.2; -; mRNA.
DR   EMBL; AK152476; BAE31250.1; -; mRNA.
DR   EMBL; AK152540; BAE31295.1; -; mRNA.
DR   EMBL; BC007187; AAH07187.1; -; mRNA.
DR   EMBL; BC017617; AAH17617.1; -; mRNA.
DR   CCDS; CCDS27122.1; -.
DR   RefSeq; NP_083056.2; NM_028780.3.
DR   RefSeq; XP_017171706.1; XM_017316217.1.
DR   AlphaFoldDB; Q9DBU0; -.
DR   BioGRID; 216520; 3.
DR   STRING; 10090.ENSMUSP00000113782; -.
DR   GlyGen; Q9DBU0; 3 sites.
DR   iPTMnet; Q9DBU0; -.
DR   PhosphoSitePlus; Q9DBU0; -.
DR   EPD; Q9DBU0; -.
DR   jPOST; Q9DBU0; -.
DR   MaxQB; Q9DBU0; -.
DR   PaxDb; Q9DBU0; -.
DR   PRIDE; Q9DBU0; -.
DR   ProteomicsDB; 259233; -.
DR   DNASU; 74140; -.
DR   Ensembl; ENSMUST00000002391; ENSMUSP00000002391; ENSMUSG00000002320.
DR   Ensembl; ENSMUST00000120041; ENSMUSP00000112893; ENSMUSG00000002320.
DR   Ensembl; ENSMUST00000121791; ENSMUSP00000112764; ENSMUSG00000002320.
DR   Ensembl; ENSMUST00000122358; ENSMUSP00000113782; ENSMUSG00000002320.
DR   GeneID; 74140; -.
DR   KEGG; mmu:74140; -.
DR   UCSC; uc007tzs.1; mouse.
DR   CTD; 10548; -.
DR   MGI; MGI:1921390; Tm9sf1.
DR   VEuPathDB; HostDB:ENSMUSG00000002320; -.
DR   eggNOG; KOG1277; Eukaryota.
DR   GeneTree; ENSGT00940000158667; -.
DR   HOGENOM; CLU_010714_0_2_1; -.
DR   InParanoid; Q9DBU0; -.
DR   OMA; EWNGDRI; -.
DR   OrthoDB; 641127at2759; -.
DR   PhylomeDB; Q9DBU0; -.
DR   TreeFam; TF328663; -.
DR   BioGRID-ORCS; 74140; 5 hits in 72 CRISPR screens.
DR   ChiTaRS; Tm9sf1; mouse.
DR   PRO; PR:Q9DBU0; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9DBU0; protein.
DR   Bgee; ENSMUSG00000002320; Expressed in right kidney and 89 other tissues.
DR   ExpressionAtlas; Q9DBU0; baseline and differential.
DR   Genevisible; Q9DBU0; MM.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0072657; P:protein localization to membrane; IBA:GO_Central.
DR   InterPro; IPR004240; EMP70.
DR   PANTHER; PTHR10766; PTHR10766; 1.
DR   Pfam; PF02990; EMP70; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasmic vesicle; Glycoprotein; Lysosome; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..606
FT                   /note="Transmembrane 9 superfamily member 1"
FT                   /id="PRO_0000034362"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        499..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        535..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        570..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        401
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        559
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        385..409
FT                   /note="VPFFLTWSVVNSVHWANGSTQALPA -> EFLSVTQCGELSALGQRFNTGAA
FT                   T (in Ref. 1; AAF98161)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   606 AA;  68928 MW;  1DDB125FA81EC47B CRC64;
     MTVLGYPRSW SCHCLPVLIL LLGIGHGPWV EGVTHYKPGD PVILYVNKVG PYHNPQETYH
     YYQLPVCCPE KIRHKSLSLG EVLDGDRMAE SLYEIRFREN VEKRILCHMQ LSSAQVEQLR
     QAIEELYYFE FVVDDLPIRG FVGYMEESGF LPHSHKIGLW THLDFHLEFH GDRIIFANVS
     VRDVKPHSLD GLRSDELLGL THTYSVRWSE TSVEHRSDRR RGDDGGFFPR TLEIHWLSII
     NSMVLVFLLV GFVAVILMRV LRNDLARYNL DEETSSGGSS DDFDQGDNGW KIIHTDVFRF
     PPYRGLLCAV LGVGAQFLAL GTGIIVMALL GMFNVHRHGA INSAAILLYA LTCCISGYVS
     SHFYRQIGGE RWVWNIILTS SLFSVPFFLT WSVVNSVHWA NGSTQALPAT TILLLLTVWL
     LVGFPLTVIG GIFGKNNASP FDAPCRTKNI AREIPPQPWY KSTVIHMTVG GFLPFSAISV
     ELYYIFATVW GREQYTLYGI LFFVFAILLS VGACISIALT YFQLSGEDYR WWWRSVLSVG
     STGLFIFLYS VFYYARRSNM SGAVQTVEFF GYSLLTGYVF FLMLGTISFF SSLKFIRYIY
     VNLKMD
 
 
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