MISS_MOUSE
ID MISS_MOUSE Reviewed; 263 AA.
AC Q9D7G9; Q7M749;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=MAPK-interacting and spindle-stabilizing protein;
DE AltName: Full=Mitogen-activated protein kinase 1-interacting protein 1;
GN Name=Mapk1ip1; Synonyms=Miss;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION, AND
RP INTERACTION WITH MAPK1.
RX PubMed=12011110; DOI=10.1083/jcb.200202052;
RA Lefebvre C., Terret M.E., Djiane A., Rassinier P., Maro B., Verlhac M.-H.;
RT "Meiotic spindle stability depends on MAPK-interacting and spindle-
RT stabilizing protein (MISS), a new MAPK substrate.";
RL J. Cell Biol. 157:603-613(2002).
CC -!- FUNCTION: Involved in the maintenance of the spindle integrity during
CC the cytostatic factor (CSF) arrest of oocytes.
CC {ECO:0000269|PubMed:12011110}.
CC -!- SUBUNIT: Interacts with MAPK1. {ECO:0000269|PubMed:12011110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12011110}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12011110}.
CC Note=Colocalizes with the spindle at discrete sites during the second
CC meiotic division.
CC -!- DEVELOPMENTAL STAGE: Expressed in ovaries and immature oocytes and two
CC cell stage embryos, then, it disappears. It is unstable during the
CC first meiotic division and accumulates only during the second meiotic
CC division. {ECO:0000269|PubMed:12011110}.
CC -!- PTM: Phosphorylated in vitro by MAPK1. {ECO:0000269|PubMed:12011110}.
CC -!- SIMILARITY: Belongs to the MISS family. {ECO:0000305}.
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DR EMBL; AK009250; BAB26168.1; -; mRNA.
DR EMBL; BC069850; AAH69850.1; -; mRNA.
DR EMBL; BK000579; DAA00064.1; -; mRNA.
DR CCDS; CCDS21949.1; -.
DR RefSeq; NP_001038948.1; NM_001045483.1.
DR RefSeq; NP_081391.1; NM_027115.2.
DR RefSeq; XP_017167778.1; XM_017312289.1.
DR AlphaFoldDB; Q9D7G9; -.
DR MINT; Q9D7G9; -.
DR STRING; 10090.ENSMUSP00000075090; -.
DR PaxDb; Q9D7G9; -.
DR PRIDE; Q9D7G9; -.
DR DNASU; 69546; -.
DR Ensembl; ENSMUST00000075667; ENSMUSP00000075090; ENSMUSG00000041775.
DR Ensembl; ENSMUST00000118810; ENSMUSP00000113813; ENSMUSG00000041775.
DR Ensembl; ENSMUST00000119664; ENSMUSP00000112631; ENSMUSG00000041775.
DR GeneID; 69546; -.
DR KEGG; mmu:69546; -.
DR UCSC; uc009kfc.1; mouse.
DR CTD; 69546; -.
DR MGI; MGI:1916796; Mapk1ip1.
DR VEuPathDB; HostDB:ENSMUSG00000041775; -.
DR eggNOG; ENOG502RYAB; Eukaryota.
DR GeneTree; ENSGT00730000111340; -.
DR HOGENOM; CLU_1057552_0_0_1; -.
DR InParanoid; Q9D7G9; -.
DR OMA; PRPNSAH; -.
DR OrthoDB; 1455063at2759; -.
DR PhylomeDB; Q9D7G9; -.
DR BioGRID-ORCS; 69546; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Mapk1ip1; mouse.
DR PRO; PR:Q9D7G9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D7G9; protein.
DR Bgee; ENSMUSG00000041775; Expressed in primary oocyte and 229 other tissues.
DR Genevisible; Q9D7G9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR031653; MISS.
DR PANTHER; PTHR35973; PTHR35973; 1.
DR Pfam; PF15822; MISS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Developmental protein; Meiosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..263
FT /note="MAPK-interacting and spindle-stabilizing protein"
FT /id="PRO_0000209888"
FT REGION 13..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..159
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 263 AA; 27761 MW; 0D8B993796E9034E CRC64;
MYPFIPPARL LPGSPAPFLP SGPSCPQPSG PYPGPAVRVP GPTRSYVSTN VPFPELPRPN
SAPTDPVGPL GTQGSMSSGP WAPGMGGQHP NVPYLFPESS PTPPLPVSGA PPVAWVTVPP
GAWEPPAQYP TPEASYPSPG LQPSPNNPYP LPPGPSAASP GPGSLHRMNE IPGGSPSDSS
NPESTLESTG QKKHLKLDNK SIKRRRSKKK SKRVTWGDIK TLTHKAESLG KQQGHNTTDP
KMMLLCLMTM LHVNSQHESE GSK
