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 27-MAR-2024, entry version 142. DE RecName: Full=Protein spinster homolog 1; DE AltName: Full=MSpin1; DE AltName: Full=Spns1 {ECO:0000303|PubMed:36161949}; 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). RN [4] RP FUNCTION, TRANSPORTER ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=36161949; DOI=10.1073/pnas.2210353119; RA He M., Kuk A.C.Y., Ding M., Chin C.F., Galam D.L.A., Nah J.M., Tan B.C., RA Yeo H.L., Chua G.L., Benke P.I., Wenk M.R., Ho L., Torta F., Silver D.L.; RT "Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid RT salvage."; RL Proc. Natl. Acad. Sci. U.S.A. 119:e2210353119-e2210353119(2022). CC -!- FUNCTION: Plays a critical role in the phospholipid salvage pathway CC from lysosomes to the cytosol (PubMed:36161949). Mediates the rate- CC limiting, proton-dependent, lysosomal efflux of lysophospholipids, CC which can then be reacylated by acyltransferases in the endoplasmic CC reticulum to form phospholipids (PubMed:36161949). Selective for CC zwitterionic headgroups such as lysophosphatidylcholine (LPC) and CC lysophosphatidylethanolamine (LPE), can also transport CC lysophosphatidylglycerol (LPG), but not other anionic CC lysophospholipids, sphingosine, nor sphingomyelin (PubMed:36161949). CC Transports lysophospholipids with saturated, monounsaturated, and CC polyunsaturated fatty acids, such as 1-hexadecanoyl-sn-glycero-3- CC phosphocholine, 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine and 1- CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine, CC respectively (PubMed:36161949). Can also transport lysoplasmalogen (LPC CC with a fatty alcohol) such as 1-(1Z-hexadecenyl)-sn-glycero-3- CC phosphocholine. Essential player in lysosomal homeostasis CC (PubMed:36161949). Crucial for cell survival under conditions of CC nutrient limitation. May be involved in necrotic or autophagic cell CC death (By similarity). {ECO:0000250|UniProtKB:Q9H2V7, CC ECO:0000269|PubMed:36161949}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine(out) + H(+)(out) = a 1- CC acyl-sn-glycero-3-phosphocholine(in) + H(+)(in); CC Xref=Rhea:RHEA:74435, ChEBI:CHEBI:15378, ChEBI:CHEBI:58168; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine(out) + H(+)(out) = CC 1-hexadecanoyl-sn-glycero-3-phosphocholine(in) + H(+)(in); CC Xref=Rhea:RHEA:74427, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(out) + CC H(+)(out) = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(in) + CC H(+)(in); Xref=Rhea:RHEA:74411, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3- CC phosphocholine(out) + H(+)(out) = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)- CC sn-glycero-3-phosphocholine(in) + H(+)(in); Xref=Rhea:RHEA:74451, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:74344; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3- CC phosphocholine(out) + H(+)(out) = 1-(4Z,7Z,10Z,13Z,16Z,19Z- CC docosahexaenoyl)-sn-glycero-3-phosphocholine(in) + H(+)(in); CC Xref=Rhea:RHEA:74423, ChEBI:CHEBI:15378, ChEBI:CHEBI:73873; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine(out) + H(+)(out) = a CC 1-acyl-sn-glycero-3-phosphoethanolamine(in) + H(+)(in); CC Xref=Rhea:RHEA:74439, ChEBI:CHEBI:15378, ChEBI:CHEBI:64381; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine(out) + CC H(+)(out) = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine(in) CC + H(+)(in); Xref=Rhea:RHEA:74415, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:74971; Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol)(out) + H(+)(out) CC = 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol)(in) + H(+)(in); CC Xref=Rhea:RHEA:74443, ChEBI:CHEBI:15378, ChEBI:CHEBI:64840; CC Evidence={ECO:0000250|UniProtKB:Q9H2V7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol)(out) CC + H(+)(out) = 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn- CC glycerol)(in) + H(+)(in); Xref=Rhea:RHEA:74419, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:72828; Evidence={ECO:0000250|UniProtKB:Q9H2V7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine(out) + H(+)(out) CC = 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine(in) + H(+)(in); CC Xref=Rhea:RHEA:74447, ChEBI:CHEBI:15378, ChEBI:CHEBI:77287; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine(out) + CC H(+)(out) = 1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine(in) + CC H(+)(in); Xref=Rhea:RHEA:74431, ChEBI:CHEBI:15378, ChEBI:CHEBI:73850; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine(out) + CC H(+)(out) = 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine(in) + CC H(+)(in); Xref=Rhea:RHEA:74455, ChEBI:CHEBI:15378, ChEBI:CHEBI:77288; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-(1Z-hexadecenyl)-sn-glycero-3-phosphoethanolamine(out) + CC H(+)(out) = 1-O-(1Z-hexadecenyl)-sn-glycero-3-phosphoethanolamine(in) CC + H(+)(in); Xref=Rhea:RHEA:74459, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:133139; Evidence={ECO:0000269|PubMed:36161949}; CC -!- SUBUNIT: Interacts with BCL2 and BCL2L1. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:36161949}; CC Multi-pass membrane protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in liver (at mRNA and protein levels). CC {ECO:0000269|PubMed:36161949}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Spinster CC (TC 2.A.1.49) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 BioGRID; 216172; 1. DR STRING; 10090.ENSMUSP00000032994; -. DR iPTMnet; Q8R0G7; -. DR PhosphoSitePlus; Q8R0G7; -. DR SwissPalm; Q8R0G7; -. DR jPOST; Q8R0G7; -. DR MaxQB; Q8R0G7; -. DR PaxDb; 10090-ENSMUSP00000032994; -. DR ProteomicsDB; 261573; -. DR Pumba; Q8R0G7; -. DR Antibodypedia; 26665; 85 antibodies from 20 providers. DR DNASU; 73658; -. DR Ensembl; ENSMUST00000032994.15; ENSMUSP00000032994.9; ENSMUSG00000030741.16. DR GeneID; 73658; -. DR KEGG; mmu:73658; -. DR UCSC; uc009jqy.3; mouse. DR AGR; MGI:1920908; -. DR CTD; 83985; -. DR MGI; MGI:1920908; Spns1. DR VEuPathDB; HostDB:ENSMUSG00000030741; -. DR eggNOG; KOG1330; Eukaryota. DR GeneTree; ENSGT00390000005976; -. DR InParanoid; Q8R0G7; -. DR OMA; TYYKEHF; -. DR OrthoDB; 4555119at2759; -. DR PhylomeDB; Q8R0G7; -. DR TreeFam; TF314395; -. DR BioGRID-ORCS; 73658; 7 hits in 80 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 228 other cell types or tissues. DR ExpressionAtlas; Q8R0G7; baseline and differential. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IMP:MGI. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro. DR GO; GO:0051977; P:lysophospholipid transport; IMP:MGI. DR GO; GO:0033700; P:phospholipid efflux; IMP:MGI. DR GO; GO:0035751; P:regulation of lysosomal lumen pH; IMP:MGI. DR CDD; cd17328; MFS_spinster_like; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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:SF13; PROTEIN SPINSTER HOMOLOG 1; 1. DR PANTHER; PTHR23505; SPINSTER; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. DR Genevisible; Q8R0G7; MM. PE 2: Evidence at transcript level; KW Acetylation; Lipid transport; Lysosome; Membrane; Phosphoprotein; KW Reference proteome; 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 //