SPNS1_DANRE
ID SPNS1_DANRE Reviewed; 506 AA.
AC Q7ZU13; Q8UVB7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein spinster homolog 1;
DE AltName: Full=Protein not really started;
DE AltName: Full=Spinster-like protein;
GN Name=spns1; Synonyms=nrs, spinl;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11836794; DOI=10.1002/dvdy.10060;
RA Young R.M., Marty S., Nakano Y., Wang H., Yamamoto D., Lin S.,
RA Allende M.L.;
RT "Zebrafish yolk-specific not really started (nrs) gene is a vertebrate
RT homolog of the Drosophila spinster gene and is essential for
RT embryogenesis.";
RL Dev. Dyn. 223:298-305(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=18704191; DOI=10.1371/journal.pgen.1000152;
RA Kishi S., Bayliss P.E., Uchiyama J., Koshimizu E., Qi J., Nanjappa P.,
RA Imamura S., Islam A., Neuberg D., Amsterdam A., Roberts T.M.;
RT "The identification of zebrafish mutants showing alterations in senescence-
RT associated biomarkers.";
RL PLoS Genet. 4:E1000152-E1000152(2008).
CC -!- FUNCTION: Sphingolipid transporter. {ECO:0000250,
CC ECO:0000269|PubMed:11836794}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in yolk cells.
CC {ECO:0000269|PubMed:11836794}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout embryogenesis, and also in adults.
CC {ECO:0000269|PubMed:11836794}.
CC -!- DISRUPTION PHENOTYPE: Presence in early embryos of an opaque substance
CC in the posterior yolk cell extension at approximately 1 day after
CC fertilization. This material progressively accumulates and by 48 hours
CC after fertilization fills the entire yolk. By day 3 of embryogenesis,
CC embryos are severely reduced in size compared with their wild-type
CC siblings and they die a few hours later. {ECO:0000269|PubMed:11836794,
CC ECO:0000269|PubMed:18704191}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Spinster (TC
CC 2.A.1.49) family. {ECO:0000305}.
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DR EMBL; AF465772; AAL69987.1; -; mRNA.
DR EMBL; BC048024; AAH48024.1; -; mRNA.
DR AlphaFoldDB; Q7ZU13; -.
DR SMR; Q7ZU13; -.
DR STRING; 7955.ENSDARP00000009970; -.
DR PaxDb; Q7ZU13; -.
DR Ensembl; ENSDART00000183172; ENSDARP00000148387; ENSDARG00000111727.
DR ZFIN; ZDB-GENE-020228-1; spns1.
DR eggNOG; KOG1330; Eukaryota.
DR InParanoid; Q7ZU13; -.
DR PhylomeDB; Q7ZU13; -.
DR PRO; PR:Q7ZU13; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR Bgee; ENSDARG00000111727; Expressed in yolk syncytial layer.
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:0097352; P:autophagosome maturation; IMP:ZFIN.
DR GO; GO:0006914; P:autophagy; IGI:ZFIN.
DR GO; GO:0090398; P:cellular senescence; IMP:ZFIN.
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 Lipid transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..506
FT /note="Protein spinster homolog 1"
FT /id="PRO_0000305041"
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 362
FT /note="M -> I (in Ref. 1; AAL69987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 54981 MW; B4168E84D2CC19BF CRC64;
MSQADADITP FFADDNEGEG PVENGVGSPL PEDEEEESPS GVTDRRAIMT VIVLCYINLL
NYMDRFTVAG VLPDIEHFFG IGDGTSGLLQ TVFICSYMFL APLFGYLGDR YNRKLIMCVG
IFFWSVVTLA SSFIGKDHFW ALLLTRGLVG VGEASYSTIA PTIIADLFVK EKRTNMLSIF
YFAIPVGSGM GYIVGSKVDT VAKDWHWALR VTPGLGLLAV FLLMLVVQEP KRGAIEAHPE
HTLHRTSWLA DMKALCRNPS FILSTFGFTA VAFVTGSLAL WAPAFLFRAG VFTGVKQPCF
KAPCDDSDSL IFGAITVVTG ILGVASGVQA SKLLRTRTPR ADPLVCAAGL LLAAPFLYLS
IMFAQASTVA TYVFIFLGET FLSMNWAIVA DILLYVVIPT RRSTAEAFQI VLSHLLGDAI
SPYLIGVVSD SIKESNSYMW EFRSLQMSLL LCSFVAVAGG AFFLATAVFI EKDRDLAENY
VPSDDAPIVV PRSGRSTKVS VSSVLI
