SPNS1_MOUSE
ID SPNS1_MOUSE Reviewed; 528 AA.
AC Q8R0G7; Q3TKM0; Q99LN7; Q9EQK0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein spinster homolog 1;
GN Name=Spns1;
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].
RX PubMed=11340170; DOI=10.1128/mcb.21.11.3775-3788.2001;
RA Nakano Y., Fujitani K., Kurihara J., Ragan J., Usui-Aoki K., Shimoda L.,
RA Lukacsovich T., Suzuki K., Sezaki M., Sano Y., Ueda R., Awano W.,
RA Kaneda M., Umeda M., Yamamoto D.;
RT "Mutations in the novel membrane protein spinster interfere with programmed
RT cell death and cause neural degeneration in Drosophila melanogaster.";
RL Mol. Cell. Biol. 21:3775-3788(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary tumor;
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=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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: Sphingolipid transporter. May be involved in necrotic or
CC autophagic cell death (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BCL2 and BCL2L1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Spinster (TC
CC 2.A.1.49) family. {ECO:0000305}.
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DR EMBL; AF212372; AAG43831.1; -; mRNA.
DR EMBL; AK166931; BAE39125.1; -; mRNA.
DR EMBL; BC002297; AAH02297.1; -; mRNA.
DR EMBL; BC026854; AAH26854.1; -; mRNA.
DR EMBL; BC085491; AAH85491.1; -; mRNA.
DR CCDS; CCDS21826.1; -.
DR RefSeq; NP_076201.2; NM_023712.3.
DR AlphaFoldDB; Q8R0G7; -.
DR SMR; Q8R0G7; -.
DR STRING; 10090.ENSMUSP00000032994; -.
DR iPTMnet; Q8R0G7; -.
DR PhosphoSitePlus; Q8R0G7; -.
DR SwissPalm; Q8R0G7; -.
DR jPOST; Q8R0G7; -.
DR MaxQB; Q8R0G7; -.
DR PaxDb; Q8R0G7; -.
DR PRIDE; Q8R0G7; -.
DR ProteomicsDB; 261573; -.
DR Antibodypedia; 26665; 80 antibodies from 20 providers.
DR DNASU; 73658; -.
DR Ensembl; ENSMUST00000032994; ENSMUSP00000032994; ENSMUSG00000030741.
DR GeneID; 73658; -.
DR KEGG; mmu:73658; -.
DR UCSC; uc009jqy.3; mouse.
DR CTD; 83985; -.
DR MGI; MGI:1920908; Spns1.
DR VEuPathDB; HostDB:ENSMUSG00000030741; -.
DR eggNOG; KOG1330; Eukaryota.
DR GeneTree; ENSGT00390000005976; -.
DR InParanoid; Q8R0G7; -.
DR OMA; VIRAMHT; -.
DR OrthoDB; 891881at2759; -.
DR PhylomeDB; Q8R0G7; -.
DR TreeFam; TF314395; -.
DR BioGRID-ORCS; 73658; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Spns1; mouse.
DR PRO; PR:Q8R0G7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R0G7; protein.
DR Bgee; ENSMUSG00000030741; Expressed in yolk sac and 225 other tissues.
DR ExpressionAtlas; Q8R0G7; baseline and differential.
DR Genevisible; Q8R0G7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd17328; MFS_spinster_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR044770; MFS_spinster-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR23505; PTHR23505; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H2V7"
FT CHAIN 2..528
FT /note="Protein spinster homolog 1"
FT /id="PRO_0000305040"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2V7"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2V7"
FT CONFLICT 60
FT /note="L -> I (in Ref. 2; BAE39125)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="R -> K (in Ref. 3; AAH02297)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="L -> F (in Ref. 1; AAG43831)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="L -> F (in Ref. 1; AAG43831)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="L -> M (in Ref. 1; AAG43831)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="L -> F (in Ref. 1; AAG43831)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="V -> M (in Ref. 1; AAG43831)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 56709 MW; DDAB448D7D2B9E17 CRC64;
MAGSDTAPFL SQADDPDDGP APGHPGLPGP MGNPKSGELE VPDCEGLQRI TGLSRGHSTL
IVVVLCYINL LNYMDRFTVA GVLTDIEQFF NIGDGSTGLI QTVFISSYMV LAPVFGYLGD
RYNRKYLMCG GIAFWSLVTL GSSFIPREHF WLLLLTRGLV GVGEASYSTI APTLIADLFV
ADQRSRMLSI FYFAIPVGSG LGYIAGSKVK DVAGDWHWAL RVTPGLGVLA VLLLFLVVQE
PPRGAVERHS GSPPLSPTSW WADLKALARN PSFVLSSLGF TSVAFVTGSL ALWAPAFLLR
SRVVLGETPP CLPGDSCSSS DSLIFGLITC LTGVLGVGLG VEISRRLRRF NPRADPLVCA
AGLLGSAPFL FLALACARGS IVATYIFIFI GETLLSMNWA IVADILLYVV IPTRRSTAEA
FQIVLSHLLG DAGSPYLIGL ISDRLRRSWP PSFLSEFRAL QFSLMLCAFV GALGGAAFLG
TAMFIEDDRR RAQLHVQGLL HESGPSDDRI VVPQRGRSTR VPVSSVLI
