KIFA3_MOUSE
ID KIFA3_MOUSE Reviewed; 793 AA.
AC P70188; P70189; Q6GTS3;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Kinesin-associated protein 3;
DE Short=KAP-3;
DE Short=KAP3;
GN Name=Kifap3;
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], PROTEIN SEQUENCE OF 86-106; 150-185 AND
RP 486-498, AND ALTERNATIVE SPLICING.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=8710890; DOI=10.1073/pnas.93.16.8443;
RA Yamazaki H., Nakata T., Okada Y., Hirokawa N.;
RT "Cloning and characterization of KAP3: a novel kinesin superfamily-
RT associated protein of KIF3A/3B.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8443-8448(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS KAP3A AND KAP3B).
RC STRAIN=C57BL/6J; TISSUE=Brain, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, 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: Involved in tethering the chromosomes to the spindle pole and
CC in chromosome movement. Binds to the tail domain of the KIF3A/KIF3B
CC heterodimer to form a heterotrimeric KIF3 complex and may regulate the
CC membrane binding of this complex.
CC -!- SUBUNIT: Interacts with SMC3 subunit of the cohesin complex (By
CC similarity). Heterotrimer of KIFAP3, KIF3A and KIF3B. Interacts with
CC RAP1GDS1/SMG GDS. {ECO:0000250}.
CC -!- INTERACTION:
CC P70188; P28741: Kif3a; NbExp=4; IntAct=EBI-6169443, EBI-6169413;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=KAP3A;
CC IsoId=P70188-1; Sequence=Displayed;
CC Name=KAP3B;
CC IsoId=P70188-2; Sequence=VSP_003899;
CC -!- PTM: Phosphorylated on tyrosine residues by SRC in vitro; this reduces
CC the binding affinity of the protein for RAP1GDS1. {ECO:0000250}.
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DR EMBL; D50366; BAA08901.1; -; mRNA.
DR EMBL; D50367; BAA08902.1; -; mRNA.
DR EMBL; BC040362; AAH40362.1; -; mRNA.
DR EMBL; BC049100; AAH49100.1; -; mRNA.
DR CCDS; CCDS35751.1; -. [P70188-2]
DR CCDS; CCDS78729.1; -. [P70188-1]
DR PIR; JC6161; JC6161.
DR RefSeq; NP_001292572.1; NM_001305643.1. [P70188-1]
DR RefSeq; NP_034759.1; NM_010629.3. [P70188-2]
DR AlphaFoldDB; P70188; -.
DR SMR; P70188; -.
DR BioGRID; 200951; 6.
DR ComplexPortal; CPX-3204; KIF3 complex variant AB-KAP3.
DR ComplexPortal; CPX-3205; KIF3 complex variant AC-KAP3.
DR CORUM; P70188; -.
DR IntAct; P70188; 8.
DR MINT; P70188; -.
DR STRING; 10090.ENSMUSP00000076830; -.
DR iPTMnet; P70188; -.
DR PhosphoSitePlus; P70188; -.
DR EPD; P70188; -.
DR jPOST; P70188; -.
DR MaxQB; P70188; -.
DR PaxDb; P70188; -.
DR PeptideAtlas; P70188; -.
DR PRIDE; P70188; -.
DR ProteomicsDB; 269308; -. [P70188-1]
DR ProteomicsDB; 269309; -. [P70188-2]
DR Antibodypedia; 20546; 185 antibodies from 26 providers.
DR DNASU; 16579; -.
DR Ensembl; ENSMUST00000027877; ENSMUSP00000027877; ENSMUSG00000026585. [P70188-1]
DR Ensembl; ENSMUST00000077642; ENSMUSP00000076830; ENSMUSG00000026585. [P70188-2]
DR GeneID; 16579; -.
DR KEGG; mmu:16579; -.
DR UCSC; uc007dho.2; mouse. [P70188-2]
DR UCSC; uc007dhp.2; mouse. [P70188-1]
DR CTD; 22920; -.
DR MGI; MGI:107566; Kifap3.
DR VEuPathDB; HostDB:ENSMUSG00000026585; -.
DR eggNOG; KOG1222; Eukaryota.
DR GeneTree; ENSGT00390000003574; -.
DR HOGENOM; CLU_009879_1_0_1; -.
DR InParanoid; P70188; -.
DR OMA; NFVEFVG; -.
DR OrthoDB; 535512at2759; -.
DR PhylomeDB; P70188; -.
DR TreeFam; TF314964; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16579; 3 hits in 59 CRISPR screens.
DR ChiTaRS; Kifap3; mouse.
DR PRO; PR:P70188; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P70188; protein.
DR Bgee; ENSMUSG00000026585; Expressed in barrel cortex and 257 other tissues.
DR Genevisible; P70188; MM.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IBA:GO_Central.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016939; C:kinesin II complex; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:1990075; C:periciliary membrane compartment; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0120170; F:intraciliary transport particle B binding; IDA:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0044782; P:cilium organization; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IPI:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:MGI.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IMP:MGI.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0046587; P:positive regulation of calcium-dependent cell-cell adhesion; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0070242; P:thymocyte apoptotic process; IMP:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR008658; KAP3.
DR PANTHER; PTHR15605; PTHR15605; 1.
DR SMART; SM00185; ARM; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..793
FT /note="Kinesin-associated protein 3"
FT /id="PRO_0000084303"
FT REPEAT 333..373
FT /note="ARM 1"
FT REPEAT 374..412
FT /note="ARM 2"
FT REPEAT 494..533
FT /note="ARM 3"
FT REPEAT 578..620
FT /note="ARM 4"
FT REPEAT 621..662
FT /note="ARM 5"
FT REGION 103..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 759..793
FT /note="LGMDGFGQPLGILGRPATAYGFRPDEPYYYSFGSR -> TVHPRISKCFASV
FT H (in isoform KAP3B)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003899"
SQ SEQUENCE 793 AA; 91291 MW; 38EBC7FD5312DAAB CRC64;
MQGEDARYLK RKVKGGNIDV HPSEKALIVQ YEVEATILGE MGDPMLGERK ECQKIIRLKS
LNANTDITSL ARKVVEECKL IHPSKLSEVE QLLYYLQNRR DSLPGKEKKE KSSKPKDPPP
FEGMEIDEVA NINDMDEYIE LLYEDIPDKV RGSALILQLA RNPDNLEELL LNETALGALA
RVLREDWKQS VELATNIIYI FFCFSSFSHF HGLITHYKIG ALCMNIIDHE LKRHELWQEE
LSKKKKAVDE DLENQTLRKD YDKTFKKYQG LVVKQEQLLR VALYLLLNLA EDTRTELKMR
NKNIVHMLVK ALDRDNFELL ILVVSFLKKL SIFMENKNDM VEMDIVEKLV KMIPCEHEDL
LNITLRLLLN LSFDTGLRNK MVQVGLLPKL TALLGNENYK QIAMCVLYHI SMDDRFKSMF
AYTDCIPQLM KMLFECSDER IDLELISFCI NLAANKRNVQ LICEGNGLKM LMKRALKLKD
PLLMKMIRNI SQHDGPTKNL FIDYVGDLAA QISSDEEEEF VIECLGTLAN LTIPDLDWEL
VLKEYKLVPF LKDKLKPGAA EDDLVLEVVI MIGTVSMDDS CAALLAKSGI IPALIELLNA
QQEDDEFVCQ IIYVFYQMVF HQATRDVIIK ETQAPAYLID LMHDKNNEIR KVCDNTLDII
AEYDEEWAKK IQSEKFRWHN SQWLEMVESR QLDESEQYLY GDDRIEPYIH EGDILERPDL
FYNSDGLITS EGAISPDFFN DFHLQNGDVV GQHAFPGSLG MDGFGQPLGI LGRPATAYGF
RPDEPYYYSF GSR
