ID G3SUG2_LOXAF Unreviewed; 1533 AA.
AC G3SUG2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Kinesin family member 13B {ECO:0000313|Ensembl:ENSLAFP00000003787.4};
GN Name=KIF13B {ECO:0000313|Ensembl:ENSLAFP00000003787.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000003787.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000003787.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003787.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000003787.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003787.4};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR STRING; 9785.ENSLAFP00000003787; -.
DR Ensembl; ENSLAFT00000004539.4; ENSLAFP00000003787.4; ENSLAFG00000004531.4.
DR eggNOG; KOG0241; Eukaryota.
DR GeneTree; ENSGT00940000155500; -.
DR InParanoid; G3SUG2; -.
DR OMA; LVCSIKI; -.
DR TreeFam; TF105221; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
DR CDD; cd22730; FHA_KIF13B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
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:SF5; -; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12473; DUF3694; 2.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT DOMAIN 1..38
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1426..1468
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 231..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1533 AA; 171174 MW; 76A558437B03699D CRC64;
DSLGGNSKTA MVATVSPAAD NYDETLSTLR YADRAKNIVN HAVVNEDPNA RIIRDLREEV
EKLREQLTKA EAMKSPELKE RLEESEKLIQ EMTVTWEEKL RKTEEIAQER QKQLESLGIS
LQSSGIKVGD DKCFLVNLNA DPALNELLVY YLKEHTLIGS ANSQDIQLCG MGILPEHCII
DITTEGQVML TPQKNTRTFV NGSCVSSPIQ LHHGDRILWG NNHFFRLNLP KKKKKAQSED
EEHDNSMKND NSSEQLDVDG DSSSEVSSEI NFNYEYAQME VTMKALGNND PMQSILKSLE
QQHEEEKRSA LERQRLMYEH ELEQLRRRLS PEKQNYRSSM DRFPFHSPSA QQRLRQWAEE
REATLNNSLM RLREQIVKAN LLVREASYIA EELDKRTEYK VTLQIPASSL DANKKRGSVL
SEPAIQVRRK GKGKQIWSLE KLDNRLLDMR DLYQEWKECE EDSPVIRSYF KRADPFYDEQ
ENHSLIGVAN VFLESLFYDV KLQYAVPIVN QKGEVAGRLH VEVMRISGEI GERIAGGDDA
VDISFDRETQ ENKLVCMVKI LQATGLPQHL SHFVFCKYNF WDQQEPMIVA PEVDTSSSPV
SKEPQCMVVF DHCNEFSVNI TEDFIEHLSE GALAIEVYGH KMTDPRKNPA VWDLGIIQAK
TRSLRDRWSE VTRKVEFWVQ ILEQNENGDY CPVEVISAKD VPTGGIFQLR QGQSRRIQVE
VKSVQESGTL PLMEECILSV GVGCIKIRPL RSPKTHETFH KCMIYLFFFQ DRDLERLRRK
WLNALTKRQE YLDQQLQKLV SKHDKTEDDA DREAQLLEMR LTLTEERNAV MVPSAGSGIP
GAPAEWTPVP GMETHIPVIF LDLNADDFSS QDNLDDPEAG GWDATLTGEE EEEFFELQIV
KQHDAEVKAE ASWDSAVHNC PQLSKGTPSD ERVFLIVRVT VQLSHPAEMQ LVLRKRICVT
VHGRQGFAQS LLKKMSHRSS IPGCGVTFEI VSNIPEDAQG VEEREALARM AANVENPASA
DSEAYIEKYL RSVLAVENLL TLDRLRQEVA VKEQLTGKGK LSRRSISSPN VNRLSGSRQD
LTPSYSLGSN KGRWESQQDV SQTVLSRGIA PGPPSLSGCP QNNHSPDPGL SSLAASYLNP
VKSFVPQMPK LLKSLFPVRD EKRGKQLSPL THQPVPRIMV QSTLLDVAVT RMEEVSLTVS
AKCKVTVQIP PVVKIYDKPA KVPSQQPLPA NAQAQEVPEG PPSPLSETSS GYFSHSVSTA
TLSDALVTGL DAASQAAPSS PPTPICQVPL ETDLSFPSVT VREPGSPKDQ MKPATSLELD
ISKPQFPPDL LSQSSAPTSP FRIQKVRTSE LKSFTRMLGG DSCSSSTEEE QLASGGSGDS
NSGGQALEKL EVVSDSEEAS EVPEWLKEGE YVTIGTNKMG IVRYIGPTDF QEGTWIGVEL
DLPSGKNDGS IGGKQYFKCN PGYGLLVKPS RVRKAMGAAR RRSTGLRLQG AAASEARRSA
TLSGSATNLA SLTALAKAER NQKSTENRKS WAS
//
