SPNS1_RAT
ID SPNS1_RAT Reviewed; 528 AA.
AC Q2YDU8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein spinster homolog 1;
GN Name=Spns1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2YDU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2YDU8-2; Sequence=VSP_036364;
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Spinster (TC
CC 2.A.1.49) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC087072; Type=Frameshift; Evidence={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; BC087072; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC110048; AAI10049.1; -; mRNA.
DR RefSeq; NP_001034297.2; NM_001039208.2. [Q2YDU8-1]
DR RefSeq; XP_017444888.1; XM_017589399.1. [Q2YDU8-1]
DR AlphaFoldDB; Q2YDU8; -.
DR SMR; Q2YDU8; -.
DR STRING; 10116.ENSRNOP00000024185; -.
DR jPOST; Q2YDU8; -.
DR PaxDb; Q2YDU8; -.
DR PRIDE; Q2YDU8; -.
DR Ensembl; ENSRNOT00000024185; ENSRNOP00000024185; ENSRNOG00000017621. [Q2YDU8-1]
DR GeneID; 361648; -.
DR KEGG; rno:361648; -.
DR UCSC; RGD:1305613; rat. [Q2YDU8-1]
DR CTD; 83985; -.
DR RGD; 1305613; Spns1.
DR eggNOG; KOG1330; Eukaryota.
DR GeneTree; ENSGT00390000005976; -.
DR HOGENOM; CLU_001265_5_12_1; -.
DR InParanoid; Q2YDU8; -.
DR OMA; VIRAMHT; -.
DR OrthoDB; 891881at2759; -.
DR PhylomeDB; Q2YDU8; -.
DR TreeFam; TF314395; -.
DR PRO; PR:Q2YDU8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017621; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q2YDU8; RN.
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; Alternative splicing; Lipid transport; Membrane;
KW Mitochondrion; Mitochondrion inner 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_0000363952"
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 VAR_SEQ 322..528
FT /note="SLIFGLITCLTGVLGVGLGVEISRRLRRFNPRADPLVCAAGLLGSSPFLFLS
FT LACARGSIVATYIFIFIGETLLSMNWAIVADILLYVVIPTRRSTAEAFQIVLSHLLGDA
FT GSPYLIGLISDRLRRSWPPSFLSEFRALQFSLMLCAFVGALGGAAFLGTAMFIENDRRR
FT AQLHVQGLLHETEPSDDQIVVPQRGRSTRVPVSSVLI -> RYL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036364"
SQ SEQUENCE 528 AA; 56796 MW; 5F098AFBD47C4AA5 CRC64;
MAGSDTAPFL SQADDPDDGP APGHPGLPGP MGNPKSGELE VPDCEGLQRI TGLSRGHSTL
IVVVLCYINL LNYMDRFTVA GVLTDIEQFF NIGDGSTGLI QTVFISSYMV LAPVFGYLGD
RYNRKYLMCG GIAFWSLVTL GSSFIPREHF WLLLLTRGLV GVGEASYSTI APTLIADLFV
ADQRSRMLSI FYFAIPVGSG LGYIAGSKVK DLAGDWHWAL RVTPGLGVLA VLLLFLVVQE
PPRGAVERHS GSPPLSPTSW WADLKALARN PSFVLSSLGF TAVAFVTGSL ALWAPAFLLR
SRVVLGETPP CLPGDSCSSS DSLIFGLITC LTGVLGVGLG VEISRRLRRF NPRADPLVCA
AGLLGSSPFL FLSLACARGS IVATYIFIFI GETLLSMNWA IVADILLYVV IPTRRSTAEA
FQIVLSHLLG DAGSPYLIGL ISDRLRRSWP PSFLSEFRAL QFSLMLCAFV GALGGAAFLG
TAMFIENDRR RAQLHVQGLL HETEPSDDQI VVPQRGRSTR VPVSSVLI
