KI13A_MOUSE
ID KI13A_MOUSE Reviewed; 1749 AA.
AC Q9EQW7; O35062;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Kinesin-like protein KIF13A;
GN Name=Kif13a;
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], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH AP2B1.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=11106728; DOI=10.1016/s0092-8674(00)00161-6;
RA Nakagawa T., Setou M., Seog D.H., Ogasawara K., Dohmae N., Takio K.,
RA Hirokawa N.;
RT "A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma
RT membrane through direct interaction with AP-1 complex.";
RL Cell 103:569-581(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 98-257.
RC STRAIN=ICR;
RX PubMed=9275178; DOI=10.1073/pnas.94.18.9654;
RA Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y.,
RA Hirokawa N.;
RT "Identification and classification of 16 new kinesin superfamily (KIF)
RT proteins in mouse genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=11374900; DOI=10.1006/geno.2001.6535;
RA Jamain S., Quach H., Fellous M., Bourgeron T.;
RT "Identification of the human KIF13A gene homologous to Drosophila kinesin-
RT 73 and candidate for schizophrenia.";
RL Genomics 74:36-44(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1477; SER-1481 AND SER-1600,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and Spleen;
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: Plus end-directed microtubule-dependent motor protein
CC involved in intracellular transport and regulating various processes
CC such as mannose-6-phosphate receptor (M6PR) transport to the plasma
CC membrane, endosomal sorting during melanosome biogenesis and
CC cytokinesis. During melanosome maturation, required for delivering
CC melanogenic enzymes from recycling endosomes to nascent melanosomes by
CC creating peripheral recycling endosomal subdomains in melanocytes. Also
CC required for the abcission step in cytokinesis: mediates translocation
CC of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis (By
CC similarity). Mediates the transport of M6PR-containing vesicles from
CC trans-Golgi network to the plasma membrane via direct interaction with
CC the AP-1 complex. {ECO:0000250, ECO:0000269|PubMed:11106728}.
CC -!- SUBUNIT: Interacts with AP1G1 and AP1G2. Interacts with ZFYVE26 (By
CC similarity). Interacts with AP2B1. {ECO:0000250,
CC ECO:0000269|PubMed:11106728}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11106728}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000305|PubMed:11106728}. Midbody
CC {ECO:0000250}. Endosome membrane {ECO:0000250}. Note=Recruited to the
CC midbody during cytokinesis. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, expressed essentially in the central
CC nervous system. Widely expressed at 10.5 dpc. At 11.5 dpc, expressed in
CC the telencephaon, otic vesicles, limb buds, nasal processes and
CC urogenital bud. {ECO:0000269|PubMed:11374900}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AB037923; BAB16346.1; -; mRNA.
DR EMBL; AB001429; BAA22389.1; -; mRNA.
DR CCDS; CCDS36652.1; -.
DR PDB; 5DJO; X-ray; 1.74 A; A/B=390-555.
DR PDBsum; 5DJO; -.
DR AlphaFoldDB; Q9EQW7; -.
DR SMR; Q9EQW7; -.
DR STRING; 10090.ENSMUSP00000055304; -.
DR iPTMnet; Q9EQW7; -.
DR PhosphoSitePlus; Q9EQW7; -.
DR EPD; Q9EQW7; -.
DR jPOST; Q9EQW7; -.
DR MaxQB; Q9EQW7; -.
DR PaxDb; Q9EQW7; -.
DR PeptideAtlas; Q9EQW7; -.
DR PRIDE; Q9EQW7; -.
DR ProteomicsDB; 263598; -.
DR MGI; MGI:1098264; Kif13a.
DR eggNOG; KOG0241; Eukaryota.
DR InParanoid; Q9EQW7; -.
DR PhylomeDB; Q9EQW7; -.
DR ChiTaRS; Kif13a; mouse.
DR PRO; PR:Q9EQW7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9EQW7; protein.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0035459; P:vesicle cargo loading; ISS:UniProtKB.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR032923; KIF13A.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR PANTHER; PTHR24115:SF458; PTHR24115:SF458; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Endosome; Golgi apparatus; Membrane; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1749
FT /note="Kinesin-like protein KIF13A"
FT /id="PRO_0000125447"
FT DOMAIN 5..352
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 469..519
FT /note="FHA"
FT REGION 633..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1584..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..431
FT /evidence="ECO:0000255"
FT COILED 552..775
FT /evidence="ECO:0000255"
FT COILED 1086..1126
FT /evidence="ECO:0000255"
FT COILED 1475..1499
FT /evidence="ECO:0000255"
FT COMPBIAS 634..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1H9"
FT MOD_RES 1274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1H9"
FT MOD_RES 1441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1H9"
FT MOD_RES 1477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1H9"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1H9"
FT CONFLICT 100
FT /note="A -> T (in Ref. 2; BAA22389)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="V -> A (in Ref. 2; BAA22389)"
FT /evidence="ECO:0000305"
FT HELIX 389..431
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 468..475
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:5DJO"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:5DJO"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:5DJO"
SQ SEQUENCE 1749 AA; 195813 MW; DAE9E026127DDBF2 CRC64;
MSDTKVKVAV RVRPMNRREL ELNTKCVVEM EGNQTVLHPP PSNTKQGERK PPKVFAFDYC
FWSMDESNTT KYAGQEVVFK CLGEGILEKA FQGYNACIFA YGQTGSGKSF SMMGHAEQLG
LIPRLCCALF QRIALEQNES QTFKVEVSYM EIYNEKVRDL LDPKGSRQSL KVREHKVLGP
YVDGLSQLAV TSFEDIESLM SEGNKSRTVA ATNMNEESSR SHAVFNIIIT QTLYDLQSGN
SGEKVSKVSL VDLAGSERVS KTGAAGERLK EGSNINKSLT TLGLVISSLA DQAAGKGKNK
FVPYRDSVLT WLLKDNLGGN SQTSMIATIS PAADNYEETL STLRYADRAK RIVNHAVVNE
DPNAKVIREL REEVEKLREQ LSKAEAMKPP ELKEKLEESE KLIKELTVTW EEKLRKTEAI
AQERQRQLES MGISLETSGI KVGDDKCYLV NLNADPALNE LLVYYLKDHT RVGADTSQDI
QLFGIGIQPE HCEIDIAADG DITLTPKENA RSCVNGTLVC NTTQLWHGDR ILWGNNHFFR
INLPKRKRRD WLKDFERETS SAEHDLDAAS EASSEPDYNY EFAQMEVIMK TLNSNDPVQN
VVQVLEKQYL EEKRTALEEQ RLMYERELEQ LRQQLSPERQ PPSSASDRLA YSSQTAQQKV
TQWAEERDEL FRQSLAKLRE QLVKANTLVR EANFLAEEMS KLTDYQVTLQ IPAANLSANR
KRGAIVSEPA IQARRKGKGT QVWTIEKLEN KLIDMRDLYQ EWKENVPEAK RLYGKRGDPF
YEAQENHNLI GVANVFLECL FCDVKLQYAV PIISQQGEVA GRLHVEVTRI TGTIPERMAE
DDSSENSSES GSLEVVDSSG EVIHRVKKLT CRVIIKEATG LPISLSNFVF CQYTFWDQCE
STVAAPVVDP DVPSPQSKDA QYTVTFSHCK DYVVTVTEEF LEFISDGALA IEVWGHRCAG
NGSPIWEVDS LHAKTRTLHD RWNEVTRRIE VWISILELNE LGDYAAVELH QAKDVNTGGV
FQLRQGHSRR VQVTVKPVQH SGTLPLMVEA ILSVSIGCVT ARSTKLQRGL DSYQEEDLNC
VRERWSDALI KRREYLDEQI KKVSNKKEKT EDDMEREARL VEQWVGLTEE RNAVLVPAPG
SGIPGAPADW VPPPGMETHI PVLFLDLNAD DLSANEQLVG PHASGVNSIL PKEHGSQFFY
LPIIKHSDDE VSATASWDSS VHDSLHLNRV TPQNERIYLI VKTTVQLSHP AAMELVLRKR
IAANIYNKQS FTQSLKRRIS LINICYSCGV TYEIVSNIPK ATEEIEDRET LALLAARSEN
EGTLDGETYI EKYTRGVLQV ENILSLERLR QAVTVKEALS TKARHIRRSL STPNVHNVSS
SRPDLSGFDE DDKGWPENQL DVSDYSSSYQ DVACYGTLPR DSPRRSKEGC PSENPHALTV
SPFKAFSPQP PKFFKPLMPV KEEHKKRLAL EARPLLSQED SEEEENELEA LSRKLMLTQP
YVPVEFADFS VYNASLENRE WSSSKADLTD SRALEKAVSR SPTTSSLTSG YFSHSASNAT
LSDMAVPSSD SSDQLAVSTK EVECAEPPGP SLAPDVRRAS NQELTEVGRG SGKDETIAVP
LEENSALPKG TPSPQSIPEE SSRMPCRTAS CSELDVGPSK DGHQAREFCP GEVTIEHTTN
ILEDHSFTEF MGVSDGKDFD GLADCSVGEP SRRRALTNET DHKGIPERPP DADRLHPKIE
NDQEATATR
