SFT2A_MOUSE
ID SFT2A_MOUSE Reviewed; 159 AA.
AC Q5SSN7; A1L3Q4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Vesicle transport protein SFT2A;
DE AltName: Full=SFT2 domain-containing protein 1;
GN Name=Sft2d1 {ECO:0000250|UniProtKB:Q8WV19};
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] {ECO:0000312|EMBL:BAE30316.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE30316.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE30316.1};
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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 [3] {ECO:0000312|EMBL:CAI25035.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH91770.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH91770.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH91770.1};
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in fusion of retrograde transport vesicles
CC derived from an endocytic compartment with the Golgi complex.
CC {ECO:0000250|UniProtKB:P38166}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SFT2 family. {ECO:0000255}.
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DR EMBL; AK151338; BAE30316.1; -; mRNA.
DR EMBL; AL663031; CAI25035.1; -; Genomic_DNA.
DR EMBL; CH466619; EDL02112.1; -; Genomic_DNA.
DR EMBL; BC091770; AAH91770.1; -; mRNA.
DR EMBL; BC130232; AAI30233.1; -; mRNA.
DR CCDS; CCDS49945.1; -.
DR RefSeq; NP_598875.2; NM_134114.2.
DR AlphaFoldDB; Q5SSN7; -.
DR IntAct; Q5SSN7; 1.
DR MINT; Q5SSN7; -.
DR STRING; 10090.ENSMUSP00000090857; -.
DR iPTMnet; Q5SSN7; -.
DR PhosphoSitePlus; Q5SSN7; -.
DR SwissPalm; Q5SSN7; -.
DR PaxDb; Q5SSN7; -.
DR PRIDE; Q5SSN7; -.
DR ProteomicsDB; 261197; -.
DR DNASU; 106489; -.
DR Ensembl; ENSMUST00000093169; ENSMUSP00000090857; ENSMUSG00000069899.
DR Ensembl; ENSMUST00000154553; ENSMUSP00000117294; ENSMUSG00000073468.
DR GeneID; 106489; -.
DR KEGG; mmu:106489; -.
DR UCSC; uc008ajm.1; mouse.
DR CTD; 113402; -.
DR MGI; MGI:1918689; Sft2d1.
DR VEuPathDB; HostDB:ENSMUSG00000069899; -.
DR VEuPathDB; HostDB:ENSMUSG00000073468; -.
DR eggNOG; KOG2887; Eukaryota.
DR GeneTree; ENSGT00390000018525; -.
DR HOGENOM; CLU_099529_2_2_1; -.
DR InParanoid; Q5SSN7; -.
DR OMA; IKCFSSC; -.
DR OrthoDB; 1476123at2759; -.
DR PhylomeDB; Q5SSN7; -.
DR TreeFam; TF315157; -.
DR BioGRID-ORCS; 106489; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Sft2d1; mouse.
DR PRO; PR:Q5SSN7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q5SSN7; protein.
DR Bgee; ENSMUSG00000069899; Expressed in morula and 52 other tissues.
DR ExpressionAtlas; Q5SSN7; baseline and differential.
DR Genevisible; Q5SSN7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR007305; Vesicle_transpt_Got1/SFT2.
DR InterPro; IPR011691; Vesicle_transpt_SFT2.
DR PANTHER; PTHR23137; PTHR23137; 1.
DR Pfam; PF04178; Got1; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..159
FT /note="Vesicle transport protein SFT2A"
FT /id="PRO_0000238608"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..62
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..122
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
SQ SEQUENCE 159 AA; 17923 MW; A64A3ED729039049 CRC64;
MEKLRRVLSG QDDEEQGLTA QVLDASSLSF NTRLKWFVIC FVAGIFFSFL GTGLLWLPNG
MKLFAVFYTL GNLAALASTC FLMGPVKQLK KMFETTRLLA TIIMLLCLVF TLCAALWWRK
KGLALLFCIL QFLSMTWYSL SYIPYARDAV LKCCSSLLG
