ST4A1_MOUSE
ID ST4A1_MOUSE Reviewed; 284 AA.
AC P63046; O88872; Q3TXY5; Q91XS5; Q9CWY7; Q9DC97;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Sulfotransferase 4A1;
DE Short=ST4A1;
DE EC=2.8.2.-;
DE AltName: Full=Brain sulfotransferase-like protein;
DE Short=mBR-STL;
DE AltName: Full=Nervous system sulfotransferase;
DE Short=NST;
GN Name=Sult4a1; Synonyms=Sultx3;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12039030; DOI=10.1016/s0378-1119(02)00431-6;
RA Sakakibara Y., Suiko M., Pai T.G., Nakayama T., Takami Y., Katafuchi J.,
RA Liu M.-C.;
RT "Highly conserved mouse and human brain sulfotransferases: molecular
RT cloning, expression, and functional characterization.";
RL Gene 285:39-47(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Visual cortex;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Atypical sulfotransferase family member with very low
CC affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low
CC catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-
CC nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in
CC the metabolism of drugs and neurotransmitters in the CNS.
CC {ECO:0000269|PubMed:12039030}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63046-1, Q9DC97-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P63046-2, Q9DC97-2;
CC Sequence=VSP_006305;
CC -!- TISSUE SPECIFICITY: Expressed in brain, cerebellum and hypothalamus.
CC Not detected in pancreas, liver, lung, intestine, kidney, uterus,
CC adrenal gland, thymus, spleen, epididymis, testicle, and heart.
CC {ECO:0000269|PubMed:12039030}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AF059257; AAC63999.1; -; mRNA.
DR EMBL; AK003034; BAB22522.1; -; mRNA.
DR EMBL; AK010293; BAB26829.1; -; mRNA.
DR EMBL; AK159034; BAE34779.1; -; mRNA.
DR EMBL; BC051132; AAH51132.1; -; mRNA.
DR EMBL; BC054757; AAH54757.1; -; mRNA.
DR CCDS; CCDS27708.1; -.
DR CCDS; CCDS88819.1; -. [P63046-2]
DR RefSeq; NP_038901.3; NM_013873.3. [P63046-1]
DR RefSeq; XP_006521128.1; XM_006521065.3.
DR AlphaFoldDB; P63046; -.
DR SMR; P63046; -.
DR BioGRID; 205926; 3.
DR STRING; 10090.ENSMUSP00000080973; -.
DR iPTMnet; P63046; -.
DR PhosphoSitePlus; P63046; -.
DR MaxQB; P63046; -.
DR PaxDb; P63046; -.
DR PeptideAtlas; P63046; -.
DR PRIDE; P63046; -.
DR ProteomicsDB; 258746; -.
DR ProteomicsDB; 258747; -. [P63046-2]
DR Antibodypedia; 304; 172 antibodies from 26 providers.
DR DNASU; 29859; -.
DR Ensembl; ENSMUST00000082365; ENSMUSP00000080973; ENSMUSG00000018865. [P63046-1]
DR Ensembl; ENSMUST00000229826; ENSMUSP00000155695; ENSMUSG00000018865. [P63046-2]
DR GeneID; 29859; -.
DR KEGG; mmu:29859; -.
DR UCSC; uc007xbs.1; mouse.
DR UCSC; uc007xbt.1; mouse. [P63046-2]
DR CTD; 25830; -.
DR MGI; MGI:1888971; Sult4a1.
DR VEuPathDB; HostDB:ENSMUSG00000018865; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000158662; -.
DR HOGENOM; CLU_027239_1_1_1; -.
DR InParanoid; P63046; -.
DR OMA; MVESCHQ; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P63046; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.1; 3474.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR BioGRID-ORCS; 29859; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Sult4a1; mouse.
DR PRO; PR:P63046; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P63046; protein.
DR Bgee; ENSMUSG00000018865; Expressed in medial dorsal nucleus of thalamus and 115 other tissues.
DR Genevisible; P63046; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR GO; GO:0140059; P:dendrite arborization; ISO:MGI.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Lipid metabolism; Phosphoprotein;
KW Reference proteome; Steroid metabolism; Transferase.
FT CHAIN 1..284
FT /note="Sulfotransferase 4A1"
FT /id="PRO_0000085168"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63047"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63047"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BR01"
FT VAR_SEQ 248..284
FT /note="GRVGLWKDIFTVSMNEKFDLVYKQKMGKCDLTFDFYL -> AHCLFTQKIAL
FT RWRGCRGSGSRLHCLDLVHVTA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_006305"
FT CONFLICT 6
FT /note="A -> R (in Ref. 2; BAB22522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 33054 MW; FCAE940F7219E6FC CRC64;
MAESEAETPG TPGEFESKYF EFHGVRLPPF CRGKMEDIAD FPVRPSDVWI VTYPKSGTSL
LQEVVYLVSQ GADPDEIGLM NIDEQLPVLE YPQPGLDIIK ELTSPRLIKS HLPYRFLPSD
LHNGDSKVIY MARNPKDLVV SYYQFHRSLR TMSYRGTFQE FCRRFMNDKL GYGSWFEHVQ
EFWEHRMDAN VLFLKYEDMH RDLVTMVEQL ARFLGVSCDK AQLESLIEHC HQLVDQCCNA
EALPVGRGRV GLWKDIFTVS MNEKFDLVYK QKMGKCDLTF DFYL
