SHSA5_MOUSE
ID SHSA5_MOUSE Reviewed; 235 AA.
AC Q9D7I0; Q8BJ86; Q8BJ87; Q8BLE9; Q8K4W3; Q91Z37; Q9CQP5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein shisa-5;
DE AltName: Full=Scotin;
DE Flags: Precursor;
GN Name=Shisa5; Synonyms=Scotin;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, INDUCTION,
RP DOMAIN, AND SUBCELLULAR LOCATION.
RC STRAIN=129/Sv, and ICR X Swiss Webster; TISSUE=Thymus;
RX PubMed=12135983; DOI=10.1083/jcb.200203006;
RA Bourdon J.-C., Renzing J., Robertson P.L., Fernandes K.N., Lane D.P.;
RT "Scotin, a novel p53-inducible proapoptotic protein located in the ER and
RT the nuclear membrane.";
RL J. Cell Biol. 158:235-246(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Colon, Corpora quadrigemina, Olfactory bulb, Retina, and Tongue;
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] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 INTERACTION WITH PDCD6.
RX PubMed=17889823; DOI=10.1016/j.abb.2007.07.028;
RA Draeby I., Woods Y.L., la Cour J.M., Mollerup J., Bourdon J.C.,
RA Berchtold M.W.;
RT "The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-
RT inducible gene product localized at the endoplasmic reticulum membrane.";
RL Arch. Biochem. Biophys. 467:87-94(2007).
CC -!- FUNCTION: Can induce apoptosis in a caspase-dependent manner and plays
CC a role in p53/TP53-dependent apoptosis. {ECO:0000269|PubMed:12135983}.
CC -!- SUBUNIT: Interacts with PDCD6; PDCD6 can stabilze SHISA5.
CC {ECO:0000269|PubMed:17889823}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12135983}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12135983}. Nucleus membrane
CC {ECO:0000269|PubMed:12135983}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9D7I0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D7I0-2; Sequence=VSP_029960;
CC Name=3;
CC IsoId=Q9D7I0-3; Sequence=VSP_029957, VSP_029961;
CC Name=4;
CC IsoId=Q9D7I0-5; Sequence=VSP_029958, VSP_029959;
CC -!- TISSUE SPECIFICITY: Spleen and thymus.
CC -!- INDUCTION: Induced in a p53/TP53-dependent manner in response to
CC cellular stress. {ECO:0000269|PubMed:12135983}.
CC -!- DOMAIN: The proline-rich region is required for endoplasmic reticulum
CC localization. {ECO:0000269|PubMed:12135983}.
CC -!- SIMILARITY: Belongs to the shisa family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32331.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AF520699; AAM74233.1; -; mRNA.
DR EMBL; AH011687; AAM74234.1; -; Genomic_DNA.
DR EMBL; AK009225; BAB26148.1; -; mRNA.
DR EMBL; AK018291; BAB31149.1; -; mRNA.
DR EMBL; AK020877; BAB32237.1; -; mRNA.
DR EMBL; AK033545; BAC28350.1; -; mRNA.
DR EMBL; AK045368; BAC32331.1; ALT_SEQ; mRNA.
DR EMBL; AK081060; BAC38125.1; -; mRNA.
DR EMBL; AK090357; BAC41183.1; -; mRNA.
DR EMBL; AK090373; BAC41188.1; -; mRNA.
DR EMBL; BC010238; AAH10238.1; -; mRNA.
DR EMBL; BC017600; AAH17600.1; -; mRNA.
DR EMBL; BC057089; AAH57089.1; -; mRNA.
DR CCDS; CCDS23543.1; -. [Q9D7I0-1]
DR CCDS; CCDS40771.1; -. [Q9D7I0-3]
DR CCDS; CCDS72309.1; -. [Q9D7I0-2]
DR CCDS; CCDS90666.1; -. [Q9D7I0-5]
DR RefSeq; NP_001271261.1; NM_001284332.1. [Q9D7I0-2]
DR RefSeq; NP_080134.1; NM_025858.3. [Q9D7I0-1]
DR RefSeq; NP_080657.1; NM_026381.5. [Q9D7I0-3]
DR AlphaFoldDB; Q9D7I0; -.
DR SMR; Q9D7I0; -.
DR IntAct; Q9D7I0; 1.
DR STRING; 10090.ENSMUSP00000107690; -.
DR iPTMnet; Q9D7I0; -.
DR PhosphoSitePlus; Q9D7I0; -.
DR PaxDb; Q9D7I0; -.
DR PeptideAtlas; Q9D7I0; -.
DR PRIDE; Q9D7I0; -.
DR Antibodypedia; 30112; 138 antibodies from 18 providers.
DR DNASU; 66940; -.
DR Ensembl; ENSMUST00000026737; ENSMUSP00000026737; ENSMUSG00000025647. [Q9D7I0-1]
DR Ensembl; ENSMUST00000112059; ENSMUSP00000107690; ENSMUSG00000025647. [Q9D7I0-2]
DR Ensembl; ENSMUST00000154184; ENSMUSP00000128901; ENSMUSG00000025647. [Q9D7I0-3]
DR Ensembl; ENSMUST00000200515; ENSMUSP00000142835; ENSMUSG00000025647. [Q9D7I0-5]
DR GeneID; 66940; -.
DR KEGG; mmu:66940; -.
DR UCSC; uc009rrm.2; mouse. [Q9D7I0-1]
DR UCSC; uc009rrn.2; mouse. [Q9D7I0-2]
DR UCSC; uc009rro.2; mouse. [Q9D7I0-5]
DR UCSC; uc009rrq.2; mouse. [Q9D7I0-3]
DR CTD; 51246; -.
DR MGI; MGI:1915044; Shisa5.
DR VEuPathDB; HostDB:ENSMUSG00000025647; -.
DR eggNOG; ENOG502S2Y4; Eukaryota.
DR GeneTree; ENSGT00390000008296; -.
DR InParanoid; Q9D7I0; -.
DR OMA; CPVFCCG; -.
DR OrthoDB; 1267386at2759; -.
DR PhylomeDB; Q9D7I0; -.
DR TreeFam; TF332572; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 66940; 2 hits in 70 CRISPR screens.
DR PRO; PR:Q9D7I0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D7I0; protein.
DR Bgee; ENSMUSG00000025647; Expressed in peripheral lymph node and 266 other tissues.
DR ExpressionAtlas; Q9D7I0; baseline and differential.
DR Genevisible; Q9D7I0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050699; F:WW domain binding; ISO:MGI.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:MGI.
DR InterPro; IPR026910; Shisa.
DR PANTHER; PTHR31395; PTHR31395; 1.
DR Pfam; PF13908; Shisa; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Endoplasmic reticulum; Membrane; Nucleus;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..235
FT /note="Protein shisa-5"
FT /id="PRO_0000312879"
FT TOPO_DOM 27..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 157..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029957"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029958"
FT VAR_SEQ 65..74
FT /note="WNEEMCPEPE -> MFLMRFLFSV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029959"
FT VAR_SEQ 74
FT /note="E -> ES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029960"
FT VAR_SEQ 104
FT /note="S -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029961"
FT CONFLICT 68
FT /note="E -> G (in Ref. 2; BAC41188)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="P -> H (in Ref. 2; BAC41188)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="A -> S (in Ref. 2; BAC41183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 25517 MW; 0262EFE8EB99BE11 CRC64;
MAAPAPSLWT LLLLLLLLPP PPGAHGELCR PFGEDNSIPV FCPDFCCGSC SNQYCCSDVL
RKIQWNEEMC PEPESRFSTP AEETPEHLGS ALKFRSSFDS DPMSGFGATV AIGVTIFVVF
IATIIICFTC SCCCLYKMCC PQRPVVTNTT TTTVVHAPYP QPQPQPVAPS YPGPTYQGYH
PMPPQPGMPA APYPTQYPPP YLAQPTGPPP YHESLAGASQ PPYNPTYMDS LKTIP
