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SIM22_HUMAN
ID   SIM22_HUMAN             Reviewed;          83 AA.
AC   K7EJ46; A0A1U9AC72; K7EIG5; K7EIH2;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2019, sequence version 2.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Small integral membrane protein 22 {ECO:0000305};
DE   AltName: Full=Cancer-associated small integral membrane open reading frame 1 {ECO:0000303|PubMed:29765154};
GN   Name=SMIM22 {ECO:0000312|HGNC:HGNC:48329};
GN   Synonyms=CASIMO1 {ECO:0000303|PubMed:29765154};
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 [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION,
RP   INTERACTION WITH CANX; DDOST AND SQLE, AND INDUCTION.
RX   PubMed=29765154; DOI=10.1038/s41388-018-0281-5;
RA   Polycarpou-Schwarz M., Gross M., Mestdagh P., Schott J., Grund S.E.,
RA   Hildenbrand C., Rom J., Aulmann S., Sinn H.P., Vandesompele J.,
RA   Diederichs S.;
RT   "The cancer-associated microprotein CASIMO1 controls cell proliferation and
RT   interacts with squalene epoxidase modulating lipid droplet formation.";
RL   Oncogene 37:4750-4768(2018).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pancreatic islet;
RA   Melton D., Meadows A., Clifton S., Hillier L., Marra M., Pape D., Wylie T.,
RA   Martin J., Blistain A., Schmitt A., Theising B., Ritter E., Ronko I.,
RA   Bennett J., Cardenas M., Gibbons M., McCann R., Cole R., Tsagareishvili R.,
RA   Williams T., Jackson Y., Bowers Y.;
RT   "WashU-Harvard pancreas EST project.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Brain, and Prostate;
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: May modulate lipid droplet formation throught interaction
CC       with SQLE. {ECO:0000269|PubMed:29765154}.
CC   -!- SUBUNIT: Interacts with CANX and DDOST (PubMed:29765154). Interacts
CC       with SQLE; this interaction modulates lipid droplet formation
CC       (PubMed:29765154). {ECO:0000269|PubMed:29765154}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Late endosome. Note=Partially colocalizedes with
CC       LAMP1 in late endosome. {ECO:0000269|PubMed:29765154}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=3;
CC         IsoId=K7EJ46-3; Sequence=Displayed;
CC       Name=2;
CC         IsoId=K7EJ46-2; Sequence=VSP_060203;
CC   -!- INDUCTION: Up-regulated in breast cancer.
CC       {ECO:0000269|PubMed:29765154}.
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DR   EMBL; KX065456; AND76299.1; -; mRNA.
DR   EMBL; CK903133; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC020663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC022385; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC035868; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC048326; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BI767985; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS59258.1; -. [K7EJ46-3]
DR   CCDS; CCDS59259.1; -. [K7EJ46-2]
DR   RefSeq; NP_001240719.1; NM_001253790.1. [K7EJ46-3]
DR   RefSeq; NP_001240720.1; NM_001253791.1. [K7EJ46-2]
DR   RefSeq; NP_001240722.1; NM_001253793.1. [K7EJ46-3]
DR   RefSeq; NP_001240723.1; NM_001253794.1. [K7EJ46-2]
DR   RefSeq; XP_011520801.1; XM_011522499.2. [K7EJ46-2]
DR   RefSeq; XP_011520802.1; XM_011522500.2. [K7EJ46-2]
DR   RefSeq; XP_011520803.1; XM_011522501.2. [K7EJ46-2]
DR   AlphaFoldDB; K7EJ46; -.
DR   SMR; K7EJ46; -.
DR   IntAct; K7EJ46; 12.
DR   STRING; 9606.ENSP00000481592; -.
DR   BioMuta; SMIM22; -.
DR   jPOST; K7EJ46; -.
DR   MassIVE; K7EJ46; -.
DR   PaxDb; K7EJ46; -.
DR   PeptideAtlas; K7EJ46; -.
DR   PRIDE; K7EJ46; -.
DR   Antibodypedia; 77901; 4 antibodies from 4 providers.
DR   DNASU; 440335; -.
DR   Ensembl; ENST00000586005.6; ENSP00000464748.1; ENSG00000267795.6. [K7EJ46-2]
DR   Ensembl; ENST00000586440.1; ENSP00000465037.1; ENSG00000267795.6. [K7EJ46-2]
DR   Ensembl; ENST00000588606.5; ENSP00000464737.1; ENSG00000267795.6. [K7EJ46-3]
DR   Ensembl; ENST00000589327.5; ENSP00000468237.1; ENSG00000267795.6. [K7EJ46-2]
DR   Ensembl; ENST00000589721.5; ENSP00000465660.1; ENSG00000267795.6. [K7EJ46-3]
DR   Ensembl; ENST00000591870.1; ENSP00000467010.1; ENSG00000267795.6. [K7EJ46-3]
DR   Ensembl; ENST00000615889.4; ENSP00000481592.1; ENSG00000267795.6. [K7EJ46-2]
DR   GeneID; 440335; -.
DR   KEGG; hsa:440335; -.
DR   MANE-Select; ENST00000586005.6; ENSP00000464748.1; NM_001253794.2; NP_001240723.1. [K7EJ46-2]
DR   UCSC; uc002cxt.4; human. [K7EJ46-3]
DR   CTD; 440335; -.
DR   DisGeNET; 440335; -.
DR   GeneCards; SMIM22; -.
DR   HGNC; HGNC:48329; SMIM22.
DR   HPA; ENSG00000267795; Tissue enhanced (intestine, pancreas, salivary gland, stomach).
DR   neXtProt; NX_K7EJ46; -.
DR   OpenTargets; ENSG00000267795; -.
DR   VEuPathDB; HostDB:ENSG00000267795; -.
DR   eggNOG; ENOG502S40K; Eukaryota.
DR   GeneTree; ENSGT00770000120884; -.
DR   HOGENOM; CLU_2573181_0_0_1; -.
DR   InParanoid; K7EJ46; -.
DR   OMA; IAHCCCH; -.
DR   OrthoDB; 1626199at2759; -.
DR   PathwayCommons; K7EJ46; -.
DR   BioGRID-ORCS; 440335; 22 hits in 986 CRISPR screens.
DR   ChiTaRS; SMIM22; human.
DR   GenomeRNAi; 440335; -.
DR   Pharos; K7EJ46; Tdark.
DR   PRO; PR:K7EJ46; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; K7EJ46; protein.
DR   Bgee; ENSG00000267795; Expressed in mucosa of transverse colon and 98 other tissues.
DR   ExpressionAtlas; K7EJ46; baseline and differential.
DR   Genevisible; K7EJ46; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR   InterPro; IPR031671; DUF4713.
DR   Pfam; PF15831; DUF4713; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..83
FT                   /note="Small integral membrane protein 22"
FT                   /id="PRO_0000424385"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          60..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         69
FT                   /note="R -> RKVSPW (in isoform 2)"
FT                   /id="VSP_060203"
SQ   SEQUENCE   83 AA;  9249 MW;  3C2F5927A97B607E CRC64;
     MAVSTEELEA TVQEVLGRLK SHQFFQSTWD TVAFIVFLTF MGTVLLLLLL VVAHCCCCSS
     PGPRRESPRK ERPKGVDNLA LEP
 
 
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