STML1_MOUSE
ID STML1_MOUSE Reviewed; 399 AA.
AC Q8CI66; Q8BLA3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Stomatin-like protein 1;
DE Short=SLP-1;
GN Name=Stoml1;
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=Corpora quadrigemina;
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 SUBCELLULAR LOCATION, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24247984; DOI=10.1113/jphysiol.2013.258657;
RA Kozlenkov A., Lapatsina L., Lewin G.R., Smith E.S.;
RT "Subunit-specific inhibition of acid sensing ion channels by stomatin-like
RT protein 1.";
RL J. Physiol. (Lond.) 592:557-569(2014).
CC -!- FUNCTION: May play a role in cholesterol transfer to late endosomes (By
CC similarity). May play a role in modulating membrane acid-sensing ion
CC channels. Can specifically inhibit proton-gated current of ASIC1
CC isoform 1. Can increase inactivation speed of ASIC3. May be involved in
CC regulation of proton sensing in dorsal root ganglions
CC (PubMed:24247984). {ECO:0000250|UniProtKB:Q9UBI4,
CC ECO:0000269|PubMed:24247984}.
CC -!- SUBUNIT: Interacts with STOM; may redistribute STOM from the plasma
CC membrane to late endosomes. {ECO:0000250|UniProtKB:Q9UBI4}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III
CC membrane protein {ECO:0000305}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:24247984}. Cell membrane
CC {ECO:0000269|PubMed:24247984}; Single-pass type III membrane protein
CC {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9UBI4}.
CC Membrane raft {ECO:0000250|UniProtKB:Q9UBI4}.
CC -!- TISSUE SPECIFICITY: Expressed in dorsal root ganglion neurons.
CC {ECO:0000269|PubMed:24247984}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
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DR EMBL; AK045820; BAC32502.1; -; mRNA.
DR EMBL; BC037074; AAH37074.1; -; mRNA.
DR CCDS; CCDS23241.1; -.
DR RefSeq; NP_081218.3; NM_026942.3.
DR AlphaFoldDB; Q8CI66; -.
DR SMR; Q8CI66; -.
DR BioGRID; 213233; 2.
DR STRING; 10090.ENSMUSP00000034883; -.
DR PhosphoSitePlus; Q8CI66; -.
DR SwissPalm; Q8CI66; -.
DR EPD; Q8CI66; -.
DR PaxDb; Q8CI66; -.
DR PRIDE; Q8CI66; -.
DR ProteomicsDB; 257495; -.
DR DNASU; 69106; -.
DR GeneID; 69106; -.
DR KEGG; mmu:69106; -.
DR UCSC; uc009pws.2; mouse.
DR CTD; 9399; -.
DR MGI; MGI:1916356; Stoml1.
DR eggNOG; KOG2621; Eukaryota.
DR eggNOG; KOG4170; Eukaryota.
DR InParanoid; Q8CI66; -.
DR OrthoDB; 1062075at2759; -.
DR PhylomeDB; Q8CI66; -.
DR BioGRID-ORCS; 69106; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8CI66; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CI66; protein.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
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:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0008200; F:ion channel inhibitor activity; IDA:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:1901586; P:negative regulation of acid-sensing ion channel activity; IDA:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
DR Gene3D; 3.30.1050.10; -; 1.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR043202; Band-7_stomatin-like.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR PANTHER; PTHR10264; PTHR10264; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
DR SUPFAM; SSF55718; SSF55718; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Endosome; Lipid transport; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..399
FT /note="Stomatin-like protein 1"
FT /id="PRO_0000094030"
FT TRANSMEM 58..78
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 288..399
FT /note="SCP2"
FT MOTIF 6..10
FT /note="Tyrosine-type lysosomal sorting signal"
FT /evidence="ECO:0000250|UniProtKB:Q9UBI4, ECO:0000255"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBI4"
FT CONFLICT 135
FT /note="D -> Y (in Ref. 1; BAC32502)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="R -> H (in Ref. 1; BAC32502)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="A -> P (in Ref. 1; BAC32502)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 42926 MW; 1951248C3693B9B2 CRC64;
MLGRSGYRAL PLGDFDRFQQ SSFGFLGSQK GCLSPEPGSV GPGADAPESW PSCLCHGLVS
VLGFLLLLLT FPISGWFALK IVPTYERMIV FRLGRIRNPQ GPGMVLLLPF IDSFQRVDLR
TRAFNVPPCK LASKDGAVLS VGADVQFRIW DPVLSVMAVK DLNTATRMTA HNAMTKALLR
RPLQEIQMEK LKIGDQLLLE INDVTRAWGL EVDRVELAVE AVLQPPQDSL TVPSLDSTLQ
QLALHLLGGS MNSAVGRVPS PGPDTLEMIN EVEPPASLAG AGAEPSPKQP VAEGLLTALQ
PFLSEALVSQ VGACYQFNVI LPSGTQSIYF LDLTTGQGRV GHGEPDGIPD VVVEMAEADL
QALLSKELRP LGAYMSGRLK VKGDLAVVMK LEAVLKALK
