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SMIM1_MOUSE
ID   SMIM1_MOUSE             Reviewed;          78 AA.
AC   P0C8K7;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Small integral membrane protein 1 {ECO:0000250|UniProtKB:B2RUZ4};
GN   Name=Smim1 {ECO:0000312|MGI:MGI:1916109};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Regulator of red blood cell formation.
CC       {ECO:0000250|UniProtKB:B3DHH5}.
CC   -!- SUBUNIT: Homooligomer; disulfide-linked.
CC       {ECO:0000250|UniProtKB:B2RUZ4}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:B2RUZ4};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:B2RUZ4}.
CC   -!- SIMILARITY: Belongs to the SMIM1 family. {ECO:0000305}.
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DR   EMBL; AK012228; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC055944; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS59664.1; -.
DR   RefSeq; NP_001157193.1; NM_001163721.1.
DR   RefSeq; NP_001157194.1; NM_001163722.1.
DR   RefSeq; XP_006539211.1; XM_006539148.3.
DR   RefSeq; XP_006539212.1; XM_006539149.3.
DR   RefSeq; XP_017175868.1; XM_017320379.1.
DR   AlphaFoldDB; P0C8K7; -.
DR   SMR; P0C8K7; -.
DR   STRING; 10090.ENSMUSP00000138605; -.
DR   iPTMnet; P0C8K7; -.
DR   PhosphoSitePlus; P0C8K7; -.
DR   SwissPalm; P0C8K7; -.
DR   jPOST; P0C8K7; -.
DR   MaxQB; P0C8K7; -.
DR   PeptideAtlas; P0C8K7; -.
DR   PRIDE; P0C8K7; -.
DR   ProteomicsDB; 261271; -.
DR   Antibodypedia; 74931; 36 antibodies from 9 providers.
DR   Ensembl; ENSMUST00000125533; ENSMUSP00000138324; ENSMUSG00000078350.
DR   Ensembl; ENSMUST00000126119; ENSMUSP00000138560; ENSMUSG00000078350.
DR   Ensembl; ENSMUST00000130175; ENSMUSP00000138675; ENSMUSG00000078350.
DR   Ensembl; ENSMUST00000132541; ENSMUSP00000138471; ENSMUSG00000078350.
DR   Ensembl; ENSMUST00000143047; ENSMUSP00000138733; ENSMUSG00000078350.
DR   Ensembl; ENSMUST00000145527; ENSMUSP00000138448; ENSMUSG00000078350.
DR   Ensembl; ENSMUST00000146054; ENSMUSP00000138605; ENSMUSG00000078350.
DR   Ensembl; ENSMUST00000182151; ENSMUSP00000138692; ENSMUSG00000078350.
DR   GeneID; 68859; -.
DR   KEGG; mmu:68859; -.
DR   UCSC; uc012dqf.1; mouse.
DR   CTD; 388588; -.
DR   MGI; MGI:1916109; Smim1.
DR   VEuPathDB; HostDB:ENSMUSG00000078350; -.
DR   eggNOG; ENOG502SASD; Eukaryota.
DR   GeneTree; ENSGT00520000060291; -.
DR   HOGENOM; CLU_2621305_0_0_1; -.
DR   InParanoid; P0C8K7; -.
DR   OMA; RWENSHP; -.
DR   OrthoDB; 1629265at2759; -.
DR   PhylomeDB; P0C8K7; -.
DR   BioGRID-ORCS; 68859; 3 hits in 70 CRISPR screens.
DR   ChiTaRS; Smim1; mouse.
DR   PRO; PR:P0C8K7; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P0C8K7; protein.
DR   Bgee; ENSMUSG00000078350; Expressed in right kidney and 190 other tissues.
DR   ExpressionAtlas; P0C8K7; baseline and differential.
DR   Genevisible; P0C8K7; MM.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   InterPro; IPR031744; SMIM1.
DR   PANTHER; PTHR38503; PTHR38503; 1.
DR   Pfam; PF15875; DUF4731; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Disulfide bond; Membrane; Phosphoprotein;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..78
FT                   /note="Small integral membrane protein 1"
FT                   /id="PRO_0000356183"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:B2RUZ4"
FT   TRANSMEM        49..69
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..78
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:B2RUZ4"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:B2RUZ4"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B2RUZ4"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B2RUZ4"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B2RUZ4"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B2RUZ4"
SQ   SEQUENCE   78 AA;  8764 MW;  397FECE02215E552 CRC64;
     MQSQESGVHY SRWDSSSRDE VSMTAMSSSE EASCYRRISQ KLCSGKLGIA MKVLGGVALF
     WIIFILGYIT GYYVHKCK
 
 
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