ID KANK3_MOUSE Reviewed; 791 AA.
AC Q9Z1P7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 145.
DE RecName: Full=KN motif and ankyrin repeat domain-containing protein 3 {ECO:0000305};
DE AltName: Full=Ankyrin repeat domain-containing protein 47;
GN Name=Kank3 {ECO:0000312|MGI:MGI:1098615};
GN Synonyms=Ankrd47, D17Ertd288e, Ng28;
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=Kidney;
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 GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=15112104; DOI=10.1007/s00335-003-2329-1;
RA Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P.,
RA Nagaraja R.;
RT "Gene content of the 750-kb critical region for mouse embryonic ectoderm
RT lethal tcl-w5.";
RL Mamm. Genome 15:265-276(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-163; SER-167;
RP SER-176 AND SER-279, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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.
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DR EMBL; AK002623; BAB22238.1; -; mRNA.
DR EMBL; AF110520; AAC97966.1; -; Genomic_DNA.
DR EMBL; AF528162; AAO17376.1; -; Genomic_DNA.
DR CCDS; CCDS28630.1; -.
DR RefSeq; NP_109622.1; NM_030697.2.
DR PDB; 6TLH; X-ray; 1.80 A; A/B=524-773.
DR PDBsum; 6TLH; -.
DR AlphaFoldDB; Q9Z1P7; -.
DR SMR; Q9Z1P7; -.
DR IntAct; Q9Z1P7; 1.
DR STRING; 10090.ENSMUSP00000040126; -.
DR iPTMnet; Q9Z1P7; -.
DR PhosphoSitePlus; Q9Z1P7; -.
DR MaxQB; Q9Z1P7; -.
DR PaxDb; 10090-ENSMUSP00000040126; -.
DR PeptideAtlas; Q9Z1P7; -.
DR ProteomicsDB; 269173; -.
DR Antibodypedia; 42728; 76 antibodies from 18 providers.
DR DNASU; 80880; -.
DR Ensembl; ENSMUST00000048560.11; ENSMUSP00000040126.5; ENSMUSG00000042099.17.
DR GeneID; 80880; -.
DR KEGG; mmu:80880; -.
DR UCSC; uc008bzq.1; mouse.
DR AGR; MGI:1098615; -.
DR CTD; 256949; -.
DR MGI; MGI:1098615; Kank3.
DR VEuPathDB; HostDB:ENSMUSG00000042099; -.
DR eggNOG; KOG0514; Eukaryota.
DR GeneTree; ENSGT00940000161178; -.
DR HOGENOM; CLU_004269_2_0_1; -.
DR InParanoid; Q9Z1P7; -.
DR OMA; SDAWVTE; -.
DR OrthoDB; 123304at2759; -.
DR PhylomeDB; Q9Z1P7; -.
DR TreeFam; TF324499; -.
DR BioGRID-ORCS; 80880; 9 hits in 78 CRISPR screens.
DR ChiTaRS; Kank3; mouse.
DR PRO; PR:Q9Z1P7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z1P7; Protein.
DR Bgee; ENSMUSG00000042099; Expressed in brain blood vessel and 236 other cell types or tissues.
DR ExpressionAtlas; Q9Z1P7; baseline and differential.
DR Genevisible; Q9Z1P7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR047184; KANK1-4.
DR InterPro; IPR021939; KN_motif.
DR PANTHER; PTHR24168; KN MOTIF AND ANKYRIN REPEAT DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR24168:SF23; KN MOTIF AND ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF12075; KN_motif; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Coiled coil; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..791
FT /note="KN motif and ankyrin repeat domain-containing
FT protein 3"
FT /id="PRO_0000244583"
FT REPEAT 606..636
FT /note="ANK 1"
FT REPEAT 640..677
FT /note="ANK 2"
FT REPEAT 679..708
FT /note="ANK 3"
FT REPEAT 712..742
FT /note="ANK 4"
FT REPEAT 746..775
FT /note="ANK 5"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..229
FT /evidence="ECO:0000255"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NY19"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NY19"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT HELIX 533..546
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 558..571
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 578..591
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 593..600
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 610..617
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 620..628
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 644..650
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 657..669
FT /evidence="ECO:0007829|PDB:6TLH"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 683..689
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 693..701
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 716..723
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 726..733
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 750..756
FT /evidence="ECO:0007829|PDB:6TLH"
FT HELIX 760..769
FT /evidence="ECO:0007829|PDB:6TLH"
SQ SEQUENCE 791 AA; 84186 MW; 6BB5307AEEDD83E6 CRC64;
MAKFVLNQNL PDLGGPPLYP GPTGSARSPS SPYSVETPYG FHLDLDFLKY VEEIERGPAS
RRTPGPPHAR RPRASRTGLA GARSPGAWTS SESLASDDGG ASGALSPGAF PGLSLPPLSP
RSLSRNPRVE HTLLETSRRL EQAQARERAL SPARAVTRSP RGSGRSSPAP NPALASPGPA
QLQLVREQMA AALRRLRELE DQARALPELQ EQVRALRAEK ARLLAGRVQP EQEVEIEARP
DKLAQLRRLT ERLATSDRGV RSRASPRAED PDGLAARRSE GALQVLDPGS RTPDGEPRTR
ETGTEVVPET REVDAQAVPE TGEAGVEVVP ETVEVDTWVT EELLGLPEAA ERELELLRTS
LEHQRGVSEL LRGRLRELEE AHEAAVTRPQ SRDVAAQTTL GCTEKTTQTE LPVENQPRPT
AGDEMAPVGI LKSIMKKKDG IPGAQSSQGP KSLQFVGVLN GEYESSSSED GNSDDEDGVA
EHPRSSSSGS DDSSGGSDAG TPGPHNDKDA GDCELETHPE LTAGREGRCE LNPRLREACI
ALNQQLNRPR GVTSRDGNAA RLVAQEWFRV SSQKRSQAES VAGVLRGVKS LGPELLAYVV
NLADGNGNTA LHYSVSHGNL AISSLLLDTG VCDVNHQNRA GYSALMLAAL TSVGQEEEDM
AVAQRLFSMG DVNAKASQTG QTALMLAISH GHQDMVAALL ECGADVNVQD ADGATALMCA
SEYGRLDTVQ LLLAQPGCDL TILDNEGTSA LAIALEAEQD EVAALLHAHL TSNHQGQSST
GSPTAKECND K
//
