ID Q6AXG6_MOUSE Unreviewed; 1202 AA.
AC Q6AXG6;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Kank1 protein {ECO:0000313|EMBL:AAH79563.1};
GN Name=Kank1 {ECO:0000313|EMBL:AAH79563.1, ECO:0000313|MGI:MGI:2147707};
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 {ECO:0000313|EMBL:AAH79563.1};
RN [1] {ECO:0000313|EMBL:AAH79563.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH79563.1};
RC TISSUE=Brain {ECO:0000313|EMBL:AAH79563.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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 [2] {ECO:0007829|PDB:5YBE}
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 923-1202.
RX PubMed=29158259; DOI=10.1074/jbc.M117.816017;
RA Weng Z., Shang Y., Yao D., Zhu J., Zhang R.;
RT "Structural analyses of key features in the KANK1KIF21A complex yield
RT mechanistic insights into the cross-talk between microtubules and the cell
RT cortex.";
RL J. Biol. Chem. 293:215-225(2018).
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DR EMBL; BC079563; AAH79563.1; -; mRNA.
DR RefSeq; NP_001335109.1; NM_001348180.1.
DR RefSeq; NP_852069.4; NM_181404.6.
DR PDB; 5YBE; X-ray; 2.11 A; A=923-1202.
DR PDBsum; 5YBE; -.
DR AlphaFoldDB; Q6AXG6; -.
DR SMR; Q6AXG6; -.
DR DNASU; 107351; -.
DR GeneID; 107351; -.
DR KEGG; mmu:107351; -.
DR AGR; MGI:2147707; -.
DR MGI; MGI:2147707; Kank1.
DR BioGRID-ORCS; 107351; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Kank1; mouse.
DR Genevisible; Q6AXG6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:2000393; P:negative regulation of lamellipodium morphogenesis; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; ISO:MGI.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0090521; P:podocyte cell migration; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISO:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; 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 PANTHER; PTHR24168; KN MOTIF AND ANKYRIN REPEAT DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR24168:SF19; KN MOTIF AND ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF12796; Ank_2; 2.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5YBE};
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT REPEAT 1011..1033
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1083..1115
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1116..1137
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 102..153
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 209..236
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 295..329
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 836..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..889
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 130796 MW; 85A877DC7A9487B7 CRC64;
METRRRLEQE RVTMQMAPGD FRRPRLASFG GMGSTSSLPS FVGSANHSSV IHQLQNGYQG
NGDYNSYVPA APTTSSMGSS VRHSPLSSGI STPVTNVSPM HLQHIREQMA IALKRLKELE
EQVRTIPVLQ VKISVLQEEK RQLASQLKSQ RASSQNEACG VRKRSYSAGN ASQLELLARA
RRGGGELYID YEEEEMESVE QSTQRIQEFR QLTADMQALE RKIQDSSCEV ASELRENGQC
PSRECKSVAV GSDENMNDVV VYHRDLRPCK DTAVGTVTET RNVGISVTEA MLGVITEADK
EIELQQQTIE ALKEKIYRLE VQLKETTHDR EMTKLKQELQ AAGSRKKVDK ATMAQPLVFS
KLVEALVPTR DQMVGSHVDT RESCVGTSVQ TSSVGTSCHP DCKNQVVGSE LPMNWWVVKE
RVAMHDQCVG RSVETCDRSV GVEVSVCETG SNTEASGSDL TLLKTNLNLK DVRSIGCGDC
SVDVIVCFPK ECTSRSMNTE AVGQEEAAVM AVPHTTDQHT STNLERVDQC TNTEAATLVE
SCTNTLLSTM DKQTSTQTVE MRTVAIGEGR VRDINPSTKT RSVGVGTVLS GNSEFDRPCA
VKTKESGVGQ INIQDNYLVG LKMRTIACGP PQLTVGLMGS RRSVGVGNEP VGELPEESPQ
PRVASGMVTG LDHYIERVQR LLAEQQTLLA ENYSELAEAF GEPHSQIGSL NSQLISTLSS
INSVMKSAST EELRNSDFQK ASLGKTTGNH LEYTCKCGGL RSGGLLNVQP SQPEVEAETA
EGKHSRGHEQ FPMQGSTLPP VNLTDDQIAT GLYVCPNNEN TLKSIMKKSD GNKDSNGAKK
NLQFIGINGG YETTSSDESS SDGSSSSESD DECDTIGYPP EEEEEEEEKD HDTRGMAEGH
HAVNIEGFKS ARVEDEVQVP ECEPEKEEIR ERYELSEKML SACNLLKYNI KDPKALASKD
MRICLNTLQH DWFRVSSQKS AVPAMVGDYI AAFEAVSPDV LRYIINMADG NGNTALHYSV
SHSNFQIVKL LLDADVCNVD HQNKAGYTPI MLAALAAVEA EKDMQVVEEL FSCGDVNAKA
SQAGQTALML AVSHGRIDMV KGLLACGADV NIQDDEGSTA LMCASEHGHV EIVKLLLAQP
GCNGHLEDND GSTALSIALE AGHKDIAVLL YAHLNFSKAQ SPSTPRLGRK TSPGPTHRGS
FD
//
