KI16B_MOUSE
ID KI16B_MOUSE Reviewed; 1312 AA.
AC B1AVY7; O35056; Q3TUD2; Q6ZPM0; Q8BZZ9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Kinesin-like protein KIF16B;
GN Name=Kif16b; Synonyms=Kiaa1590;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 101-239.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-1312.
RC STRAIN=C57BL/6J; TISSUE=Gonad;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 487-1161.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582 AND SER-838, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RAB14.
RX PubMed=21238925; DOI=10.1016/j.devcel.2010.11.008;
RA Ueno H., Huang X., Tanaka Y., Hirokawa N.;
RT "KIF16B/Rab14 molecular motor complex is critical for early embryonic
RT development by transporting FGF receptor.";
RL Dev. Cell 20:60-71(2011).
CC -!- FUNCTION: Plus end-directed microtubule-dependent motor protein
CC involved in endosome transport and receptor recycling and degradation.
CC Regulates the plus end motility of early endosomes and the balance
CC between recycling and degradation of receptors such as EGF receptor
CC (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome
CC transport of FGFR-containing vesicles during early development, a key
CC process for developing basement membrane and epiblast and primitive
CC endoderm lineages during early postimplantation development.
CC {ECO:0000269|PubMed:21238925}.
CC -!- SUBUNIT: Interacts with PTPN21 (By similarity). Interacts with RAB14.
CC {ECO:0000250, ECO:0000269|PubMed:21238925}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q96L93}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q96L93}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96L93}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q96L93}. Note=It is unclear whether association
CC with endosomes is mediated via phosphatidylinositol 3-phosphate
CC (PtdIns(3)P)-binding or via its interaction with RAB14.
CC {ECO:0000250|UniProtKB:Q96L93}.
CC -!- DOMAIN: The PX domain mediates binding to phosphatidylinositol 3-
CC phosphate (PtdIns(3)P), phosphatidylinositol 3,4-bisphosphate
CC (PtdIns(3,4)P2), phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2)
CC and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). Does
CC not bind phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic death. Embryos are arrested at the
CC blastocyst stage: the primitive endoderm and epiblast cannot be
CC distinguished and appear as cell clumps resembling the inner cell mass
CC (ICM) of the blastocyst. Embryos do not develop an epiblast epithelium
CC and the uterine reaction appears to be incomplete. Development of the
CC primitive endoderm and a basement membrane derived from it are severely
CC affected in embryos at 4.5 dpc. {ECO:0000269|PubMed:21238925}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98211.1; Type=Miscellaneous discrepancy; Note=Partially unspliced pre-RNA.; Evidence={ECO:0000305};
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DR EMBL; AL731712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB001423; BAA22383.1; -; mRNA.
DR EMBL; AK033018; BAC28130.2; -; mRNA.
DR EMBL; AK160835; BAE36039.1; -; mRNA.
DR EMBL; AK129401; BAC98211.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS38251.1; -.
DR RefSeq; NP_001074602.1; NM_001081133.2.
DR AlphaFoldDB; B1AVY7; -.
DR SMR; B1AVY7; -.
DR BioGRID; 200933; 3.
DR STRING; 10090.ENSMUSP00000042551; -.
DR iPTMnet; B1AVY7; -.
DR PhosphoSitePlus; B1AVY7; -.
DR EPD; B1AVY7; -.
DR MaxQB; B1AVY7; -.
DR PaxDb; B1AVY7; -.
DR PeptideAtlas; B1AVY7; -.
DR PRIDE; B1AVY7; -.
DR ProteomicsDB; 263599; -.
DR Antibodypedia; 24366; 108 antibodies from 16 providers.
DR Ensembl; ENSMUST00000043589; ENSMUSP00000042551; ENSMUSG00000038844.
DR GeneID; 16558; -.
DR KEGG; mmu:16558; -.
DR UCSC; uc008mpz.1; mouse.
DR CTD; 55614; -.
DR MGI; MGI:1098240; Kif16b.
DR VEuPathDB; HostDB:ENSMUSG00000038844; -.
DR eggNOG; KOG0245; Eukaryota.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00940000162977; -.
DR HOGENOM; CLU_001485_35_0_1; -.
DR InParanoid; B1AVY7; -.
DR OMA; HWHGAQQ; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; B1AVY7; -.
DR TreeFam; TF105221; -.
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; 16558; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Kif16b; mouse.
DR PRO; PR:B1AVY7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; B1AVY7; protein.
DR Bgee; ENSMUSG00000038844; Expressed in submandibular gland and 255 other tissues.
DR ExpressionAtlas; B1AVY7; baseline and differential.
DR Genevisible; B1AVY7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005819; C:spindle; ISO: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:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0007492; P:endoderm development; IMP:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0001704; P:formation of primary germ layer; IMP:UniProtKB.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0032801; P:receptor catabolic process; ISS:UniProtKB.
DR GO; GO:0001919; P:regulation of receptor recycling; ISS:UniProtKB.
DR Gene3D; 3.30.1520.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
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 InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00787; PX; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Endosome; Lipid-binding;
KW Membrane; Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..1312
FT /note="Kinesin-like protein KIF16B"
FT /id="PRO_0000409500"
FT DOMAIN 3..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN ?480..?544
FT /note="FHA"
FT DOMAIN 1177..1291
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT COILED 366..425
FT /evidence="ECO:0000255"
FT COILED 835..913
FT /evidence="ECO:0000255"
FT COILED 941..1073
FT /evidence="ECO:0000255"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L93"
FT MOD_RES 577
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96L93"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1047
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L93"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
SQ SEQUENCE 1312 AA; 150058 MW; 4397E49FF4E93881 CRC64;
MASVKVAVRV RPMNRREKDL EAKFIIQMEK SKTTITNLKI PEGGTGDSGR ERTKTFTYDF
SFYSADTKSP DYVSQEMVFK TLGTDVVKSA FEGYNACVFA YGQTGSGKSY TMMGNSGDSG
LIPRICEALF SRINETTRWD EASFRTEVSY LEIYNERVRD LLRRKSSKTF NLRVREHPKE
GPYVEDLSKH LVQNYSDVEE LMDAGNINRT TAATGMNDVS SRSHAIFTIK FTQAKFDAEM
PCETVSKIHL VDLAGSERAD ATGATGVRLK EGGNINKSLV TLGNVISALA DLSQDAANPL
VKKKQVFVPY RDSVLTWLLK DSLGGNSKTI MIATISPADV NYGETLSTLR YANRAKNIIN
KPTINEDANV KLIRELRAEI ARLKTLLAQG NQIALLDSPT ALSMEEKLHQ NEARVQELTK
EWTNKWNETQ NILKEQTLAL RKEGIGVVLD SELPHLIGID DDLLSTGIIL YHLKEGQTYV
GREDASTEQD IVLHGLDLES EHCVFENAGG TVTLIPLRGS QCSVNGVQIV DATQLNQGAV
ILLGRTNMFR FNHPKEAAKL REKRKSGLLS SFSLSMTDLS KSCENLSAVM LYNPGLEFER
QQREELEKLE SKRKLIEEME EKQKSDKAEL ERMQQEVETR RKETEIVQRQ IRKQEESLKR
RSFHIENKLK DLLAEKERFE EERLREQQGL EQQRRQEEES LFRIREELRK LQELNSHEQA
EKVQIFQELD RLHQEQNAQS AKLRLEKRRL EEEEKEQVQR VAHLEEQLRK RQDTAPLLCP
GEAQRAQEEK RELESIREAL LQAKEMRAGG DHTCRDELER AQQYFLEFKR RQLVKLASLE
KDLVQQKDLL SKEVQEEKVA LEHVKCDAGG DPSFLATDDG NILGGPPDLD KIKTAETRLQ
SREHQLQDLL QNHLPALLEE KQRVLDALDS GVLGLDTTLC QVEKEVGEKE EQIAQYQANA
SQLQQLRATF EFTANVARQE EKVRRKEKEI LESQEKQQRE ALEQAVAKLE QRRSALQRCS
TLDLEIQEQR QKLGSLHTSE WSGWQASLET DGEALEMDPA RLEHEIHQLK QKICEVDGVQ
RPHHGILEGQ AVLSSLPPSG GNSHLAPLMD ARISAYIEEE VQRRLHDLHR AIGDANHTPA
DVMKSNEELH NGTTQRKLKY ERMYSRSLGT NRDDLKDPIK ISIPRYVLCG QGKDEHFEFE
VKISVLDETW TVFRRYSRFR EMHKTLKLKY AELAALEFPP KKLFGNKDER VVAERRTHLE
KYLREFFSVM LQSETSPLHI NKVGLTLSKH TICEFSPFFK KGVFDYSSHG TG
