KIF12_MOUSE
ID KIF12_MOUSE Reviewed; 642 AA.
AC Q9D2Z8; O35061;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Kinesin-like protein KIF12;
GN Name=Kif12;
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=Cecum;
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 [GENOMIC DNA].
RA Matthews L.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-268.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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; AK018598; BAB31300.1; -; mRNA.
DR EMBL; AL691496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB001428; BAA22388.1; -; mRNA.
DR CCDS; CCDS18249.1; -.
DR RefSeq; NP_034746.1; NM_010616.3.
DR AlphaFoldDB; Q9D2Z8; -.
DR SMR; Q9D2Z8; -.
DR STRING; 10090.ENSMUSP00000030042; -.
DR iPTMnet; Q9D2Z8; -.
DR PhosphoSitePlus; Q9D2Z8; -.
DR PaxDb; Q9D2Z8; -.
DR PRIDE; Q9D2Z8; -.
DR ProteomicsDB; 263529; -.
DR Antibodypedia; 15422; 77 antibodies from 21 providers.
DR DNASU; 16552; -.
DR Ensembl; ENSMUST00000030042; ENSMUSP00000030042; ENSMUSG00000028357.
DR GeneID; 16552; -.
DR KEGG; mmu:16552; -.
DR UCSC; uc008tfq.1; mouse.
DR CTD; 113220; -.
DR MGI; MGI:1098232; Kif12.
DR VEuPathDB; HostDB:ENSMUSG00000028357; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000161216; -.
DR HOGENOM; CLU_001485_2_1_1; -.
DR InParanoid; Q9D2Z8; -.
DR OMA; RWNKTQG; -.
DR PhylomeDB; Q9D2Z8; -.
DR TreeFam; TF324584; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16552; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9D2Z8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D2Z8; protein.
DR Bgee; ENSMUSG00000028357; Expressed in right kidney and 47 other tissues.
DR ExpressionAtlas; Q9D2Z8; baseline and differential.
DR Genevisible; Q9D2Z8; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IDA:MGI.
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; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR028763; Kif12.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR24115; PTHR24115; 1.
DR PANTHER; PTHR24115:SF418; PTHR24115:SF418; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 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 ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..642
FT /note="Kinesin-like protein KIF12"
FT /id="PRO_0000125445"
FT DOMAIN 25..360
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 376..465
FT /evidence="ECO:0000255"
FT COMPBIAS 537..552
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FN5"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FN5"
FT CONFLICT 100..103
FT /note="VFTF -> IFAY (in Ref. 3; BAA22388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 70706 MW; 57D3F37B759EE31F CRC64;
MEERGSPDGD PARNLEQGPE GSETPIQVVL RVRPMSTVEL RRGEQSALHC SGTRTLQVSP
DVAFRFGAVL DGARTQEDVF RACGVKRLGE LALRGFSCTV FTFGQTGSGK TYTLTGPPPQ
GEGVPVPPSL AGIMQRTFTW LLDRVQHLDS PVTLRASYLE IYNEQVWDLL SLGSPRPLPV
RWTKARGFYV EQLRVVEFGS LEALMELLQM GLSRRRSSSH TLNQASSRSH ALLTLHISRP
TSQQVPPVDL GEPPVGGKLC FVDLAGSEKV AATGSQGQLM LEANSINRSL LALGHCISLL
LDPQRKQNHI PFRDSKLTKL LADSLGGRGV TLMVACVSPS AQCLPETLST LRYASRAQRI
TTRPQGPKSP GVKPPQQVEN ELLRLQEENR HLRFQLDQMH TTAPGAHGAR MAWAQRNLYG
MLQEFMLENE RLRKEMRQLR SSRDLARAEQ RVLAQQVHDL ERRLLSACPL PQQGSTPVCP
CRMVPAASCH ALPPLCYCHH FCPLCRVPLA HWTCPRRECH MPQVLEPEAP GHISQSVWPP
PWAPPPSPGS AKPPRERSQS DWTQTRVLAE MLMGEEVVPS APPLSAGPSN MPYGLRGGSG
IPNLTPRLET LTQQINSSLH LSQRQPQPSE DTQSPGQGLS SC