ID   D3YTR6_MOUSE            Unreviewed;       476 AA.
AC   D3YTR6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   04-NOV-2026, entry version 80.
DE   RecName: Full=Protein spinster homolog 1 {ECO:0000256|ARBA:ARBA00039482};
DE   AltName: Full=Spns1 {ECO:0000256|ARBA:ARBA00041462};
GN   Name=Spns1 {ECO:0000313|Ensembl:ENSMUSP00000112954.2,
GN   ECO:0000313|MGI:MGI:1920908};
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 {ECO:0000313|Ensembl:ENSMUSP00000112954.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000112954.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112954.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG   Mouse Genome Sequencing Consortium;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000112954.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112954.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=21750661;
RA   Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA   Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA   Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA   Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA   Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA   Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA   Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT   "Modernizing reference genome assemblies.";
RL   PLoS Biol. 9:e1001091-e1001091(2011).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000112954.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112954.2};
RG   Ensembl;
RL   Submitted (JUL-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine(out) +
CC         H(+)(out) = a 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine(in) +
CC         H(+)(in); Xref=Rhea:RHEA:74447, ChEBI:CHEBI:15378, ChEBI:CHEBI:77287;
CC         Evidence={ECO:0000256|ARBA:ARBA00047765};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine(out) +
CC         H(+)(out) = a 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:0000256|ARBA:ARBA00048915};
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:0000256|ARBA:ARBA00035932};
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:0000256|ARBA:ARBA00036238};
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane
CC       {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004155}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Spinster
CC       (TC 2.A.1.49) family. {ECO:0000256|ARBA:ARBA00024338}.
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DR   AlphaFoldDB; D3YTR6; -.
DR   SMR; D3YTR6; -.
DR   jPOST; D3YTR6; -.
DR   PeptideAtlas; D3YTR6; -.
DR   ProteomicsDB; 371828; -.
DR   Antibodypedia; 26665; 87 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000119846.9; ENSMUSP00000112954.2; ENSMUSG00000030741.17.
DR   AGR; MGI:1920908; -.
DR   MGI; MGI:1920908; Spns1.
DR   VEuPathDB; HostDB:ENSMUSG00000030741; -.
DR   GeneTree; ENSGT00390000005976; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000030741; Expressed in yolk sac and 228 other cell types or tissues.
DR   ExpressionAtlas; D3YTR6; baseline and differential.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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.
PE   1: Evidence at protein level;
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:D3YTR6,
KW   ECO:0007829|ProteomicsDB:D3YTR6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        57..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        304..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        329..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        371..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        410..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..476
FT                   /note="Major facilitator superfamily (MFS) profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50850"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  51396 MW;  A4DB3555CECC2F48 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 LIFGLITCLT GVLGVGLGVE ISRRLRRFNP
     RADPLVCAAG LLGSAPFLFL ALACARGSIV ATYIFIFIGE TLLSMNWAIV ADILLYVVIP
     TRRSTAEAFQ IVLSHLLGDA GSPYLIGLIS DRLRRSWPPS FLSEFRALQF SLMLCAFVGA
     LGGAAFLGTA MFIEDDRRRA QLHVQGLLHE SGPSDDRIVV PQRGRSTRVP VSSVLI
//