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IPP_MOUSE
ID   IPP_MOUSE               Reviewed;         584 AA.
AC   P28575; Q3V2M0;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 3.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Actin-binding protein IPP;
DE   AltName: Full=Intracisternal A particle-promoted polypeptide;
DE            Short=IPP;
DE   AltName: Full=Murine IAP-promoted placenta-expressed protein;
DE   AltName: Full=Protein MIPP;
GN   Name=Ipp; Synonyms=Mipp;
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].
RC   STRAIN=BALB/cJ;
RX   PubMed=11536049; DOI=10.1038/sj.onc.1204701;
RA   VanHouten J.N., Asch H.L., Asch B.B.;
RT   "Cloning and characterization of ectopically expressed transcripts for the
RT   actin-binding protein MIPP in mouse mammary carcinomas.";
RL   Oncogene 20:5366-5372(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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 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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 355-556.
RX   PubMed=1906605; DOI=10.1093/nar/19.13.3667;
RA   Chang-Yeh A., Mold D.E., Huang R.C.C.;
RT   "Identification of a novel murine IAP-promoted placenta-expressed gene.";
RL   Nucleic Acids Res. 19:3667-3672(1991).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=1905535; DOI=10.1016/0006-291x(91)90646-o;
RA   Mold D.E., Chang-Yeh A., Huang R.C.;
RT   "Cell lineage-specific expression of the MIPP gene.";
RL   Biochem. Biophys. Res. Commun. 177:1062-1067(1991).
CC   -!- FUNCTION: May play a role in organizing the actin cytoskeleton.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Expression seems confined to tissues derived from
CC       trophectoderm and primitive endoderm. {ECO:0000269|PubMed:1905535}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK00278.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA41413.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA41414.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF285178; AAK00278.1; ALT_FRAME; mRNA.
DR   EMBL; AK131718; BAE20777.1; -; mRNA.
DR   EMBL; AL669953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X58523; CAA41413.1; ALT_FRAME; mRNA.
DR   EMBL; X58524; CAA41414.1; ALT_FRAME; Genomic_DNA.
DR   CCDS; CCDS38851.1; -.
DR   PIR; S16442; S16442.
DR   RefSeq; NP_032415.2; NM_008389.3.
DR   AlphaFoldDB; P28575; -.
DR   SMR; P28575; -.
DR   BioGRID; 200781; 1.
DR   STRING; 10090.ENSMUSP00000102088; -.
DR   iPTMnet; P28575; -.
DR   PhosphoSitePlus; P28575; -.
DR   EPD; P28575; -.
DR   PaxDb; P28575; -.
DR   PRIDE; P28575; -.
DR   ProteomicsDB; 301661; -.
DR   Antibodypedia; 32715; 70 antibodies from 17 providers.
DR   DNASU; 16351; -.
DR   Ensembl; ENSMUST00000030461; ENSMUSP00000030461; ENSMUSG00000028696.
DR   Ensembl; ENSMUST00000106479; ENSMUSP00000102088; ENSMUSG00000028696.
DR   GeneID; 16351; -.
DR   KEGG; mmu:16351; -.
DR   UCSC; uc008ugp.1; mouse.
DR   CTD; 3652; -.
DR   MGI; MGI:96581; Ipp.
DR   VEuPathDB; HostDB:ENSMUSG00000028696; -.
DR   eggNOG; KOG4441; Eukaryota.
DR   GeneTree; ENSGT00940000158629; -.
DR   HOGENOM; CLU_004253_14_1_1; -.
DR   InParanoid; P28575; -.
DR   OMA; QAAYNWI; -.
DR   OrthoDB; 938011at2759; -.
DR   PhylomeDB; P28575; -.
DR   TreeFam; TF329218; -.
DR   BioGRID-ORCS; 16351; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Ipp; mouse.
DR   PRO; PR:P28575; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P28575; protein.
DR   Bgee; ENSMUSG00000028696; Expressed in secondary oocyte and 202 other tissues.
DR   Genevisible; P28575; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.80; -; 2.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR017096; BTB-kelch_protein.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR030104; IPP.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR24412:SF35; PTHR24412:SF35; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 6.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 6.
DR   SUPFAM; SSF117281; SSF117281; 2.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Kelch repeat; Reference proteome;
KW   Repeat.
FT   CHAIN           1..584
FT                   /note="Actin-binding protein IPP"
FT                   /id="PRO_0000119076"
FT   DOMAIN          37..104
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REPEAT          296..343
FT                   /note="Kelch 1"
FT   REPEAT          344..390
FT                   /note="Kelch 2"
FT   REPEAT          391..437
FT                   /note="Kelch 3"
FT   REPEAT          439..485
FT                   /note="Kelch 4"
FT   REPEAT          487..533
FT                   /note="Kelch 5"
FT   REPEAT          535..583
FT                   /note="Kelch 6"
FT   CONFLICT        6..7
FT                   /note="CP -> YA (in Ref. 1; AAK00278)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        12
FT                   /note="N -> S (in Ref. 1; AAK00278)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="S -> T (in Ref. 1; AAK00278)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="S -> K (in Ref. 1; AAK00278)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164..165
FT                   /note="VH -> SI (in Ref. 1; AAK00278)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   584 AA;  65216 MW;  BE8CE11A53F7CFED CRC64;
     MSKEECPKAA DNSFSSDKHA QLILAQMNKM RSGQHFCDVQ LQVGKETFQV HRLVLAASSP
     YFAALFTGGM KESSKDVVQI LGVEAGIFQL LLDFIYTGVV NIAVTNVQEL IVAADMLQLT
     EVVNLCCDFL KGQIDPQNCI GLFQFSEQIA CHDLLEFTEN YIHVHFLEVH TGEEFLGLTK
     DQLIKILRSE ELSIEDEYQV FLAAMQWILK DLGKRRKHVV EVLDPVRFPL LPSQRLLKYI
     EGVSDFNLRV ALQTLLKEYC EVCKSPKENK FCSFLQTSKV RPRKKARKYL YAVGGYTRLQ
     GGRWSDSRAL SCVERFDTFS QYWTTVSSLH QARCGLGVAV VGGMVYAIGG EKDSMIFDCT
     ECYDPVTKQW TTVASMNHPR CGLGVCVCYG AIYALGGWVG AEIGNTIERF DPDENKWEVV
     GSMAVSRYYF GCCEMQGLIY AVGGISNEGL ELRSFEVYDP LSKRWSPLPP MGTRRAYLGV
     AALNDCIYAI GGWNETQDAL HTVEKYSFEE EKWVEVASMK VPRAGMCAVT VNGLLYVSGG
     RSSSHDFLAP GTLDSVEVYN PHSDTWTEIG NMITSRCEGG VAVL
 
 
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