SRR1L_MOUSE
ID SRR1L_MOUSE Reviewed; 249 AA.
AC Q8K2M3; Q08AU8; Q9CSK3;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 4.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=SRR1-like protein;
DE AltName: Full=SRR1 domain-containing protein;
GN Name=Srrd;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 126-249 (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-249 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28802827; DOI=10.1016/j.abb.2017.08.006;
RA Adachi Y., Umeda M., Kawazoe A., Sato T., Ohkawa Y., Kitajima S., Izawa S.,
RA Sagami I., Taketani S.;
RT "The novel heme-dependent inducible protein, SRRD regulates heme
RT biosynthesis and circadian rhythms.";
RL Arch. Biochem. Biophys. 631:19-29(2017).
CC -!- FUNCTION: Plays a role in the regulation of heme biosynthesis and in
CC the regulation of the expression of core clock genes.
CC {ECO:0000269|PubMed:28802827}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28802827}.
CC Note=Also found in intracellular organelles.
CC {ECO:0000269|PubMed:28802827}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K2M3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K2M3-2; Sequence=VSP_038445;
CC -!- INDUCTION: Up-regulated by hemin and 5-aminolevulinic acid.
CC {ECO:0000269|PubMed:28802827}.
CC -!- SIMILARITY: Belongs to the SRR1 family. {ECO:0000305}.
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DR EMBL; AC123848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030678; AAH30678.1; -; mRNA.
DR EMBL; BC125007; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK012640; BAB28374.1; -; mRNA.
DR CCDS; CCDS51614.1; -. [Q8K2M3-1]
DR RefSeq; NP_081599.2; NM_027323.2. [Q8K2M3-1]
DR AlphaFoldDB; Q8K2M3; -.
DR STRING; 10090.ENSMUSP00000031289; -.
DR PhosphoSitePlus; Q8K2M3; -.
DR MaxQB; Q8K2M3; -.
DR PaxDb; Q8K2M3; -.
DR PRIDE; Q8K2M3; -.
DR ProteomicsDB; 262695; -. [Q8K2M3-1]
DR ProteomicsDB; 262696; -. [Q8K2M3-2]
DR Antibodypedia; 287; 81 antibodies from 18 providers.
DR Ensembl; ENSMUST00000031289; ENSMUSP00000031289; ENSMUSG00000029346. [Q8K2M3-1]
DR GeneID; 70118; -.
DR KEGG; mmu:70118; -.
DR UCSC; uc008ysz.2; mouse. [Q8K2M3-1]
DR CTD; 402055; -.
DR MGI; MGI:1917368; Srrd.
DR VEuPathDB; HostDB:ENSMUSG00000029346; -.
DR eggNOG; KOG3131; Eukaryota.
DR GeneTree; ENSGT00390000003948; -.
DR HOGENOM; CLU_062516_0_1_1; -.
DR InParanoid; Q8K2M3; -.
DR OMA; WKCVCYG; -.
DR OrthoDB; 1590454at2759; -.
DR PhylomeDB; Q8K2M3; -.
DR TreeFam; TF323595; -.
DR BioGRID-ORCS; 70118; 19 hits in 74 CRISPR screens.
DR ChiTaRS; Srrd; mouse.
DR PRO; PR:Q8K2M3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K2M3; protein.
DR Bgee; ENSMUSG00000029346; Expressed in internal carotid artery and 202 other tissues.
DR ExpressionAtlas; Q8K2M3; baseline and differential.
DR Genevisible; Q8K2M3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0070453; P:regulation of heme biosynthetic process; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR012942; SRR1-like.
DR InterPro; IPR040044; SRR1L.
DR PANTHER; PTHR28626; PTHR28626; 1.
DR Pfam; PF07985; SRR1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Biological rhythms; Cytoplasm; Heme biosynthesis;
KW Reference proteome.
FT CHAIN 1..249
FT /note="SRR1-like protein"
FT /id="PRO_0000186124"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 249
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038445"
FT CONFLICT 36
FT /note="E -> D (in Ref. 3; BAB28374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 27502 MW; 435D0871473EBCF7 CRC64;
MAAAALEPWS AVAPRRRKRA AGRRPRPGEG PRAEPEADGE AVLRRLREAE EDLRISDFCS
SALETITECL RKQLEQLQPL TEALGRLHLG SSLPSASQEP LASSASHVKC VCYGLGTFAS
CPTARIQLAF MLLFLEKCQV PRSHCWVYDP LFSQTEVSVL TSLGVTVLSE NEEGKRSVQG
QPTVFYMPHC GTALYNNLLW SNWSADALSR VLIIGNSFRG LEERLLARIL QENYPYIAKV
SDRIAGPGF
