ID A0A2I3STF0_PANTR Unreviewed; 1392 AA.
AC A0A2I3STF0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Kinesin family member 16B {ECO:0000313|Ensembl:ENSPTRP00000079845.1};
GN Name=KIF16B {ECO:0000313|Ensembl:ENSPTRP00000079845.1,
GN ECO:0000313|VGNC:VGNC:6178};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000079845.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000079845.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000079845.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; AACZ04064917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04064918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04064919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04064920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04064921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016792957.1; XM_016937468.1.
DR Ensembl; ENSPTRT00000095011.1; ENSPTRP00000079845.1; ENSPTRG00000013269.6.
DR VGNC; VGNC:6178; KIF16B.
DR GeneTree; ENSGT00940000162977; -.
DR InParanoid; A0A2I3STF0; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000002277; Chromosome 20.
DR Bgee; ENSPTRG00000013269; Expressed in pituitary gland and 21 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd22732; FHA_KIF16B; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000253; FHA_dom.
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; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT DOMAIN 3..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1036..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..421
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 599..807
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 836..867
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 942..1022
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1036..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1392 AA; 159693 MW; 2A0871F6F6B13367 CRC64;
MASVKVAVRV RPMNRREKDL EAKFIIQMEK SKTTITNLKI PEGGTGDSGR ERTKTFTYDF
SFYSADTKSP DYVSQEMVFK TLGTDVVKSA FEGYNACVFA YGQTGSGKSY TMMGNSGDSG
LIPRICEGLF SRINETTRWD EASFRTEVSY LEIYNERVRD LLRRKSSKTF NLRVREHPKE
GPYVEDLSKH LVQNYGDVEE LMDAGNINRT TAATGMNDVS SRSHAIFTIK FTQAKFDSEM
PCETVSKIHL VDLAGSERAD ATGATGVRLK EGGNINKSLV TLGNVISALA DLSQDAANTL
AKKKQVFVPY RDSVLTWLLK DSLGGNSKTI MIATISPADV NYGETLSTLR YANRAKNIIN
KPTINEDANV KLIRELRAEI ARLKTLLAQG NQIALLDSPT ALSMEEKLQQ NEARVQELTK
EWTNKWNETQ NILKEQTLAL RKEGIGVVLD SELPHLIGID DDLLSTGIIL YHLKEGQTYV
GRDDASTEQD IVLHGLDLES EHCIFENIGG TVTLIPLSGS QCSVNGVQIV EATHLNQGAV
ILLGRTNMFR FNHPKEAAKL REKRKSGLLS SFSLSMTDLS KSRENLSAVM LYNPGLEFER
QQREELEKLE SKRKLIEEME EKQKSDKAEL ERMQQEVETQ RKETEIVQLQ IRKQEESLKR
RSFHIENKLK DLLAEKEKFE EERLREQQEI ELQKKRQEEE TFLRVQEELQ RLKELNNNEK
AEKFQIFQEL DQLQKEKDEQ YAKLELEKKR LEEQEKEQVM LVAHLEEQLR EKQEMIQLLR
RGEVQWVEEE KRDLEGIRES LLQVKEARAG GDEDGEELEK AQLRFFEFKR RQLVKLVNLE
KDLVQQKDIL KKEVQEEQEI LECLKCEHDK ESRLLEKHDE SVTDVTEVAQ DFEKIKPVEY
RLQYKERQLQ YLLQNHLPTL LEEKQRAFEI LDRGPLSLDN TLYQVEKEME EKEEQLAQYQ
ANANQLQKLQ ATFEFTANIA RQEEKVRKKE KEILESREKQ QREALERALA RLERRHSALQ
RRSTLGMEIE EQRQKLASLN SGSREQSGLQ ASLEAEQEAL GKDQERLKYE IQQLKQKIYE
VDGVQKGHHG TLEGKVASSS LPVSAEKSHL VPLMDARINA YIEEEVQRRL QDLHRVINEG
CSTSADTMKD NEKLHNGTIQ RKLKYELCRD LLCVLMPEPD AAACANHPLL QQDLVQLSLD
WKTEIPDLVL PNGVQVSSKF QTTLVDMIYF LHGNMEVNVP SLAEVQLLLY TTVKVMGDSG
HDQCQSLVLL NTHIALVKED CVFYPRIRSR NIPPPGAQFD VIKCHALSEF RCVVVPEKKN
VSTVELVFLQ KLKPSVGSRN SPPEHLQEAP DVQLFTTPLY LQGSQNVAPE VWKLTFNSQD
EALWLISHLT RL
//
