LOCUS       NP_076201                528 aa            linear   ROD 10-DEC-2024
DEFINITION  protein spinster homolog 1 [Mus musculus].
ACCESSION   NP_076201
VERSION     NP_076201.2
DBSOURCE    REFSEQ: accession NM_023712.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Beenken,A., Shen,T., Jin,G., Ghotra,A., Xu,K., Nesanir,K.,
            Sturley,R.E., Vijayakumar,S., Khan,A., Levitman,A., Stauber,J.,
            Chavez,E.Y., Robbins-Juarez,S.Y., Hao,L., Field,T.B.,
            Erdjument-Bromage,H., Neubert,T.A., Shapiro,L., Qiu,A. and
            Barasch,J.
  TITLE     Spns1 is an iron transporter essential for megalin-dependent
            endocytosis
  JOURNAL   Am J Physiol Renal Physiol 327 (5), F775-F787 (2024)
   PUBMED   39265081
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Ha,H.T., Liu,S., Nguyen,X.T., Vo,L.K., Leong,N.C., Nguyen,D.T.,
            Balamurugan,S., Lim,P.Y., Wu,Y., Seong,E., Nguyen,T.Q., Oh,J.,
            Wenk,M.R., Cazenave-Gassiot,A., Yapici,Z., Ong,W.Y., Burmeister,M.
            and Nguyen,L.N.
  TITLE     Lack of SPNS1 results in accumulation of lysolipids and lysosomal
            storage disease in mouse models
  JOURNAL   JCI Insight 9 (8), e175462 (2024)
   PUBMED   38451736
  REMARK    GeneRIF: Lack of SPNS1 results in accumulation of lysolipids and
            lysosomal storage disease in mouse models.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 528)
  AUTHORS   He,M., Kuk,A.C.Y., Ding,M., Chin,C.F., Galam,D.L.A., Nah,J.M.,
            Tan,B.C., Yeo,H.L., Chua,G.L., Benke,P.I., Wenk,M.R., Ho,L.,
            Torta,F. and Silver,D.L.
  TITLE     Spns1 is a lysophospholipid transporter mediating lysosomal
            phospholipid salvage
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2210353119 (2022)
   PUBMED   36161949
  REMARK    GeneRIF: Spns1 is a lysophospholipid transporter mediating
            lysosomal phospholipid salvage.
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Yanagisawa,H., Ishii,T., Endo,K., Kawakami,E., Nagao,K.,
            Miyashita,T., Akiyama,K., Watabe,K., Komatsu,M., Yamamoto,D. and
            Eto,Y.
  TITLE     L-leucine and SPNS1 coordinately ameliorate dysfunction of
            autophagy in mouse and human Niemann-Pick type C disease
  JOURNAL   Sci Rep 7 (1), 15944 (2017)
   PUBMED   29162837
  REMARK    GeneRIF: SPNS1-dependent L-leucine export across the lysosomal
            membrane is a key step for triggering autophagy, and that this
            mechanism is impaired in Niemann-Pick type C disease-1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Nakano,Y., Fujitani,K., Kurihara,J., Ragan,J., Usui-Aoki,K.,
            Shimoda,L., Lukacsovich,T., Suzuki,K., Sezaki,M., Sano,Y., Ueda,R.,
            Awano,W., Kaneda,M., Umeda,M. and Yamamoto,D.
  TITLE     Mutations in the novel membrane protein spinster interfere with
            programmed cell death and cause neural degeneration in Drosophila
            melanogaster
  JOURNAL   Mol Cell Biol 21 (11), 3775-3788 (2001)
   PUBMED   11340170
  REMARK    GeneRIF: Spinster protein interferes with programmed cell death in
            Drosophila melanogaster and has orthologs in nematode, mouse, and
            human.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY731880.1, AF212372.1, AK166931.1 and CR519967.1.
            
            On Mar 22, 2008 this sequence version replaced NP_076201.1.
            
            Transcript Variant: This variant (1) represents a protein-coding
            transcript for this gene.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026854.1, AK166931.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 69.01 cM"
     Protein         1..528
                     /product="protein spinster homolog 1"
                     /note="spinster-like protein; spinster homolog 1; MSpin1"
                     /calculated_mol_wt=56578
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2V7; propagated from
                     UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Region          62..479
                     /region_name="MFS_spinster_like"
                     /note="Protein spinster and spinster homologs of the Major
                     Facilitator Superfamily of transporters; cd17328"
                     /db_xref="CDD:340886"
     Site            order(72..73,76..77,80,112,164..165,167..169,172,192,
                     195..196,199,280,283..284,287..289,292,333,337,390..391,
                     395,399,419,422..423,426..427,430)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            357..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            421..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            465..485
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0G7.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2V7; propagated from
                     UniProtKB/Swiss-Prot (Q8R0G7.1)"
     CDS             1..528
                     /gene="Spns1"
                     /gene_synonym="2210013K02Rik; Spin1; Spinl"
                     /coded_by="NM_023712.3:858..2444"
                     /db_xref="CCDS:CCDS21826.1"
                     /db_xref="GeneID:73658"
                     /db_xref="MGI:MGI:1920908"
ORIGIN      
        1 magsdtapfl sqaddpddgp apghpglpgp mgnpksgele vpdceglqri tglsrghstl
       61 ivvvlcyinl lnymdrftva gvltdieqff nigdgstgli qtvfissymv lapvfgylgd
      121 rynrkylmcg giafwslvtl gssfiprehf wlllltrglv gvgeasysti aptliadlfv
      181 adqrsrmlsi fyfaipvgsg lgyiagskvk dvagdwhwal rvtpglgvla vlllflvvqe
      241 pprgaverhs gspplsptsw wadlkalarn psfvlsslgf tsvafvtgsl alwapafllr
      301 srvvlgetpp clpgdscsss dslifglitc ltgvlgvglg veisrrlrrf npradplvca
      361 agllgsapfl flalacargs ivatyififi getllsmnwa ivadillyvv iptrrstaea
      421 fqivlshllg dagspyligl isdrlrrswp psflsefral qfslmlcafv galggaaflg
      481 tamfieddrr raqlhvqgll hesgpsddri vvpqrgrstr vpvssvli
//
