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SHSA2_MOUSE
ID   SHSA2_MOUSE             Reviewed;         295 AA.
AC   Q8QZV2; Q0NZZ5; Q8BN61;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Protein shisa-2 homolog;
DE   AltName: Full=Shisa-like protein 2;
DE            Short=mShisa;
DE   AltName: Full=Transmembrane protein 46;
DE   Flags: Precursor;
GN   Name=Shisa2; Synonyms=Shisa, Tmem46;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Czech II;
RX   PubMed=16773659; DOI=10.1002/dvdy.20862;
RA   Filipe M., Goncalves L., Bento M., Silva A.C., Belo J.A.;
RT   "Comparative expression of mouse and chicken Shisa homologues during early
RT   development.";
RL   Dev. Dyn. 235:2567-2573(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17481602; DOI=10.1016/j.ydbio.2007.03.028;
RA   Furushima K., Yamamoto A., Nagano T., Shibata M., Miyachi H., Abe T.,
RA   Ohshima N., Kiyonari H., Aizawa S.;
RT   "Mouse homologues of Shisa antagonistic to Wnt and Fgf signalings.";
RL   Dev. Biol. 306:480-492(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=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).
CC   -!- FUNCTION: Plays an essential role in the maturation of presomitic
CC       mesoderm cells by individual attenuation of both FGF and WNT signaling.
CC       {ECO:0000269|PubMed:16773659, ECO:0000269|PubMed:17481602}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 5.5 dpc in the distal visceral
CC       endoderm. Expression increases at 6.5 dpc in the most anterior part of
CC       the visceral endoderm. At 7.0 dpc expression spreads over the anterior
CC       visceral endoderm and occurs in the anterior ectoderm. At 7.75 dpc
CC       expressed in the definitive anterior endoderm, anterior mesoderm and
CC       anterior neuroectoderm. At 8.25 dpc, when the headfold is formed,
CC       expressed in the forebrain, foregut and in segmented somites. At 12.5
CC       dpc, expressed in cerebrum cortex, lateral ganglionic eminences,
CC       preoptic area neuroepithelium, hypothalamus, ventral part of otic
CC       placode including adjacent mesenchyme, a part of the tongue,
CC       endocardial cushion around aortic valve, myotome and muscle primordia.
CC       {ECO:0000269|PubMed:16773659, ECO:0000269|PubMed:17481602}.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit no defects in head development. Mice
CC       are live-born. About one-third of the homozygous mutants were normal
CC       and fertile and about two-thirds were dwarf. Reduction in weight gain
CC       became apparent at the postnatal third week; about half of the dwarf
CC       mice subsequently resumed the weight increase, although they remained
CC       dwarf; the other died within a month after birth.
CC       {ECO:0000269|PubMed:17481602}.
CC   -!- SIMILARITY: Belongs to the shisa family. {ECO:0000305}.
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DR   EMBL; DQ342342; ABC69144.1; -; mRNA.
DR   EMBL; AB280737; BAF57482.1; -; mRNA.
DR   EMBL; AK034905; BAC28876.1; -; mRNA.
DR   EMBL; AK087512; BAC39906.1; -; mRNA.
DR   EMBL; BC024118; AAH24118.1; -; mRNA.
DR   EMBL; BC057640; AAH57640.1; -; mRNA.
DR   CCDS; CCDS27173.1; -.
DR   RefSeq; NP_663438.1; NM_145463.5.
DR   AlphaFoldDB; Q8QZV2; -.
DR   SMR; Q8QZV2; -.
DR   STRING; 10090.ENSMUSP00000059391; -.
DR   iPTMnet; Q8QZV2; -.
DR   PhosphoSitePlus; Q8QZV2; -.
DR   PaxDb; Q8QZV2; -.
DR   PRIDE; Q8QZV2; -.
DR   ProteomicsDB; 257164; -.
DR   Antibodypedia; 53427; 57 antibodies from 10 providers.
DR   DNASU; 219134; -.
DR   Ensembl; ENSMUST00000053949; ENSMUSP00000059391; ENSMUSG00000044461.
DR   GeneID; 219134; -.
DR   KEGG; mmu:219134; -.
DR   UCSC; uc007uer.2; mouse.
DR   CTD; 387914; -.
DR   MGI; MGI:2444716; Shisa2.
DR   VEuPathDB; HostDB:ENSMUSG00000044461; -.
DR   eggNOG; ENOG502QWT7; Eukaryota.
DR   GeneTree; ENSGT00940000157443; -.
DR   HOGENOM; CLU_085916_0_0_1; -.
DR   InParanoid; Q8QZV2; -.
DR   OMA; YAHPVSP; -.
DR   OrthoDB; 1325567at2759; -.
DR   PhylomeDB; Q8QZV2; -.
DR   TreeFam; TF330800; -.
DR   BioGRID-ORCS; 219134; 1 hit in 74 CRISPR screens.
DR   ChiTaRS; Shisa2; mouse.
DR   PRO; PR:Q8QZV2; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q8QZV2; protein.
DR   Bgee; ENSMUSG00000044461; Expressed in optic fissure and 235 other tissues.
DR   Genevisible; Q8QZV2; 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:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:MGI.
DR   InterPro; IPR026910; Shisa.
DR   PANTHER; PTHR31395; PTHR31395; 1.
DR   Pfam; PF13908; Shisa; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000250"
FT   CHAIN           34..295
FT                   /note="Protein shisa-2 homolog"
FT                   /id="PRO_0000022616"
FT   TOPO_DOM        34..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          87..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        40
FT                   /note="G -> V (in Ref. 3; BAC39906)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   295 AA;  31466 MW;  59B83ECDBEE1AD7B CRC64;
     MWGGRCSPST SSRHRASLLQ LLLAALLAAG ARASGEYCHG WLDAQGVWRI GFQCPERFDG
     GDATICCGSC ALRYCCSSAE ARLDQGGCDN DRQQGVGEPG RTDREGPDSS AVPIYVPFLI
     VGSVFVAFII LGSLVAACCC RCLRPKQDPQ QSRAPGANRL METIPMIPSA STSRGSSSRQ
     SSTAASSSSS ANSGARAPPT RSQTNCCLPE GTMNNVYVNM PTNFSVLNCQ QATQIVPHQG
     QYLHTPYVGY AVQHDSVPMT PVPPFMDGLQ PGYRPVQPPF AHTNSEQKMF PAVTV
 
 
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