KANK4_MOUSE
ID KANK4_MOUSE Reviewed; 1016 AA.
AC Q6P9J5; Q8BV03;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=KN motif and ankyrin repeat domain-containing protein 4;
DE AltName: Full=Ankyrin repeat domain-containing protein 38;
GN Name=Kank4; Synonyms=Ankrd38;
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=Head;
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 STRAIN=FVB/N; TISSUE=Salivary 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-639, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in the control of cytoskeleton formation by
CC regulating actin polymerization. {ECO:0000250|UniProtKB:Q5T7N3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5T7N3}.
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DR EMBL; AK081525; BAC38246.1; -; mRNA.
DR EMBL; BC060737; AAH60737.1; -; mRNA.
DR CCDS; CCDS18379.1; -.
DR RefSeq; NP_766460.2; NM_172872.3.
DR AlphaFoldDB; Q6P9J5; -.
DR SMR; Q6P9J5; -.
DR BioGRID; 232421; 1.
DR IntAct; Q6P9J5; 1.
DR MINT; Q6P9J5; -.
DR STRING; 10090.ENSMUSP00000099851; -.
DR iPTMnet; Q6P9J5; -.
DR PhosphoSitePlus; Q6P9J5; -.
DR MaxQB; Q6P9J5; -.
DR PaxDb; Q6P9J5; -.
DR PeptideAtlas; Q6P9J5; -.
DR PRIDE; Q6P9J5; -.
DR ProteomicsDB; 301728; -.
DR Antibodypedia; 2864; 30 antibodies from 13 providers.
DR DNASU; 242553; -.
DR Ensembl; ENSMUST00000102790; ENSMUSP00000099851; ENSMUSG00000035407.
DR GeneID; 242553; -.
DR KEGG; mmu:242553; -.
DR UCSC; uc008tuk.2; mouse.
DR CTD; 163782; -.
DR MGI; MGI:3043381; Kank4.
DR VEuPathDB; HostDB:ENSMUSG00000035407; -.
DR eggNOG; KOG0514; Eukaryota.
DR GeneTree; ENSGT00940000158468; -.
DR HOGENOM; CLU_004269_0_0_1; -.
DR InParanoid; Q6P9J5; -.
DR OMA; VCDGTFG; -.
DR OrthoDB; 98668at2759; -.
DR PhylomeDB; Q6P9J5; -.
DR TreeFam; TF324499; -.
DR BioGRID-ORCS; 242553; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Kank4; mouse.
DR PRO; PR:Q6P9J5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6P9J5; protein.
DR Bgee; ENSMUSG00000035407; Expressed in sciatic nerve and 151 other tissues.
DR Genevisible; Q6P9J5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR021939; KN_motif.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF12075; KN_motif; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW ANK repeat; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1016
FT /note="KN motif and ankyrin repeat domain-containing
FT protein 4"
FT /id="PRO_0000244365"
FT REPEAT 838..868
FT /note="ANK 1"
FT REPEAT 877..905
FT /note="ANK 2"
FT REPEAT 910..939
FT /note="ANK 3"
FT REPEAT 943..973
FT /note="ANK 4"
FT REPEAT 977..1007
FT /note="ANK 5"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..409
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..652
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 639
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 282
FT /note="P -> A (in Ref. 1; BAC38246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1016 AA; 110404 MW; 522174CCE563D154 CRC64;
MEKIDGKDQS SQGDEEKEPP KSYPYSVETP YGFHLDLDFL KYVDDIEKGH TIKRIPIHRR
AKQAKFSTLP RNFSLPNSGD RTYAVPPQQN WSPVVPRKIS LGTQEPSQPL PLGDLPQASV
QGSELNYHRK ALLAKDARQA EAGSLEDVGS GRPQLLRASS MPATLLQNQV PEEPSLTSGP
STLLALPLLQ DEGSVCDGAF DPAEGLMGFQ ASAQSVDREL GELEPAIPEQ VWEGAEPEEG
DLKASSHLSQ PGPSSAVQSV PMDLEEVEIE HHMREAELVL TPGSATPSPP PLPSPILEND
LSLDEIELSI SEIPPPPPIE VDVRSIGIRV TEESLGLLET DTSSISSLKN QVLALEDKLS
GRTEELARVR AALEQQEEET KAREQRIQEL ECTVAHLEEK LSQERASEAP DRTDATVNTD
PLQELTPRES HDKNIGVNLL NTPDPECRAP RAEKNGFPWV QNNHKQSYPS PEEPVLPPQL
SLPRGPEQIL ASSLCSCLSM ELRIEEEGSE QEGGQEEGAG GLSRAAGESS WSTRESAPVI
REEATSELPG AERPGRPASS PQDATIGQYV KKIQELLHEQ WNCLEHGYPE LASAIKQPAS
KLSSIQNQLL SSLNLLLSAY SAQAPEPEPK ETPAPPPSTP PPPPPPPPEI SPSTSLKSIM
KKKDYGFRAG GNGTKKNLQF VGVNGGYETT SSEETSGEDS SPEDLSDSET EKKQDCSESR
EDRDLHPSCE AGQGVPEGTR NSGHTSDRGE EVSHLRAERY KPSEEFLNAC QTLSQHLPET
GDTTKQLLRQ SLNTISQEWF RVSSRKLSSP EAVAAYLLEV QPHSPYLLKL LVNLADRSGN
TALHYSVSHS NFAIVKLLLD TGVCNVDHQN KAGYTAVMIT PLASAETKED MAVVWKLLRE
GNVNIQATQG GQTALMLGVS HDREDMVQAL LSCQADVNLQ DNDGSSALML ACHQGNADLV
RLLLAHPACN SSLTDKAGRT ALSLVLNSPA HVEIAELLRA HSEPGRSLGP KELQKN