ID A0A1L8FAG1_XENLA Unreviewed; 3952 AA.
AC A0A1L8FAG1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=StAR-related lipid transfer protein 9 isoform X1 {ECO:0000313|RefSeq:XP_018086551.1};
GN Name=stard9.L {ECO:0000313|RefSeq:XP_018086551.1,
GN ECO:0000313|Xenbase:XB-GENE-995223};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018086551.1};
RN [1] {ECO:0000313|RefSeq:XP_018086551.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018086551.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018086551.1};
RG RefSeq;
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 RefSeq; XP_018086551.1; XM_018231062.2.
DR STRING; 8355.A0A1L8FAG1; -.
DR PaxDb; 8355-A0A1L8FAG1; -.
DR GeneID; 378631; -.
DR KEGG; xla:378631; -.
DR AGR; Xenbase:XB-GENE-995223; -.
DR CTD; 378631; -.
DR Xenbase; XB-GENE-995223; stard9.L.
DR OMA; QPHCELQ; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 378631; Expressed in spleen and 18 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22731; FHA_KIF16A_STARD9; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.530.20; -; 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 InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR PANTHER; PTHR47117:SF1; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF01852; START; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50848; START; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT REGION 300..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2555..2587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2640..2663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3050..3077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3146..3183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3380..3410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3506..3535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3626..3716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3571..3601
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 913..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3154..3177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3380..3394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3395..3409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3507..3528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3626..3650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3680..3705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 3952 AA; 440986 MW; A8C163DFFBC8F4D4 CRC64;
MANVKVALRV RPPSKRETAE GSRIILNVDE KVARIKNIRL DHKPDGCEDT RERLIEFGFD
SCYWSVDPED PKYASQEMVF QDLGTLVLSE AISGYNVCLF AYGQTGSGKT YTMMGTPASI
GLTPRICEGL FSYDEGSPET PNSFRVEVSF LEIYNERVRD LLHKSEEKKP YTLRVREHPE
RGPYVQGLSQ HVVTSYEQVV ALLEEGMENR ITAATHIHDA SSRSHAIFTI QYTQAMLEDN
LPTEITSKIN LVDLAGSERA SPEYCKDRLT EGSNINRSLV TLGIVISTLA QNSQMTSSCQ
SINSIASDGD SGSPSGGSTN GSKRQPYVPY RDSILTWLLK DSLGGNSKTI MIATVSPASS
SYNETMSTLR YASHAKNIVN KPRVNEDANV KLIRDLREEI NRLKNMIQSF EIRTISPSFS
DEKDGNFNEL VKQNELKIER LTKDWTEKWT DKEAIMEKYN VDISQGKAGL TIDSNLPYLI
AMDDDILSTR VVIYQLKEGN TNIGRCDSEQ DQDIALQGEW IEREHCMIHN CSGVVELQPV
QGAQCTINGQ EVTEACRLSQ GDVLVIGKTH RFRFNNPAEA ALLRQRRSDS QVSFVSSSSL
DWLDLSGDFS TPSNENKLIL NRNTESEDYQ QKLRDLESFY QQQVQQQQLY VEDLKKQIQT
SKIRSEKELE LEQSLINQIV EENKQWLIKE EQRLTESHHQ RRESSVQTEP KFIAEAEVQN
TAATDSYPSA VEVDRKRLVQ RELLRKCSLR RAERNIRRKR IKFQLERIIK KQKLLEAKKD
LQHLQAVCWI SEDTVKQLHN PDSEGPSKGV TRFKQSAFPC SFQTLPNLGT LKRKCAPAVS
LHSNKPSEEQ KPRRAVSVEC LSSTCCSGLL SETPNYDQCT VQGAEKHPFV SVTNQNKTST
YGKFVLAYTQ MSKKRQKMDK SGSRSKSISK TTEPLKKRNS RIPITTANSE TKLKPFKSSP
QQTLESRRKS FVQENKTTLE KNEATGKQKN TKNIQKTVPP GKRFAERSSS TLKGSKREAD
SCLPNSHKKP ANEFSKISSS TDSINTLSRP TTTHAIDKRW QSTERLSRGL LKPKEVLLQD
WKEDDETGSS DSESFYSVDS LSSAYGYALT KELHLKGPGI KKNVTSQNNS DSEDSEISQD
SLAERGTKKE KPNRRRFNNY KTVLTPCSSS KDMIEDPNPS PVVMGTSVTT GLSKSFSLDS
LADAEDVPEM DSSEEMPAEI FWKLQSPRIL GLHTDDQNNI GFPQAENRSD KGLGSSFYLN
VNPLFALDCS DSILSRSDVI HVQAQANVED AVSEKLENSC PPVLVASSLW ESQDCTITTA
NNTCEDSKTE FPNQLSTKYS TIKNEPENVD SNRMFTISPQ DTTLLNEKIQ SPIERTVEET
SVNIPLLNKN EESESTVPEF TTEQRENGCQ ILDAAANPDF KDLQYLGPLK DQLNAGENVI
LRCSVKDESR ALKDPHISVG LLTANNEDSA GLAATTGKLK AGMVKEILPT RLKMTIVNAK
KSPKKMKLMR NKDTEEMMLQ MKQNDGLTHG ASLDKNEKCE TGPFSLHVTQ GNWDTSHCNH
STTEKTFDQQ ADQDTKVAKP MPNCEQFKHT DNLETLFNHT MSKVLEEDKR ENFKMEPSPP
TSVDPEGAKM EAHSDTFDPH KLIPSSVHTP LHVELDINAN TKNCEKYVIE NDECDNGITE
SRERPNERSG STGVERIVIV PGNHPHFAVD SCVNKLSKCP SLTQDKITSV DMTMGSVEKN
TEDNAPRLHE PKSTNNLLIT NSGDLNFNQL SSRLSQANDN SFITYVSLKD AEKESGKDGA
IRPENVSVVS IESDHCFTLS SPAISRDTLN SNVSSTSLSD QGMFQGTFSL IKSIDSSLLP
SFNEGACIQV DNNMENIVKH EKDNIYRQHD ADIPIHFENV SKERREKILD GGAATEQKIS
SAKSTYGQIA PIRNHSSVPE EMTSSVKNKQ DNATVATKKA STLEKMGTLI SKGEMEMADS
MSYTLHSTDG TQDWQNDGMK ASAETTLEVS GHLCSKMNDL SQTHNKNSVA CGKLEFPSKN
YRDKNNMENQ SSSDDINALW ASGSANNPLY QDVQCFPVPN ICESGEKTSN GITSSCSSRS
GNRTNPAEDV RNAGLVLPYY EAVLQNELLN EAKNTADKIL NSEPFMKKGK AEASPVSSEN
NKSCSGAKSL VKPQVQCSIQ LDIHSTCANA PSETRTPSIP TDATFMFEGA SVPVIPNNTS
HFVYGNESCV DKPLEKGASS QDIPKRTPFI SQQHSSCPAK NSELLSKNNK LEPDSSSKLR
YFQSRTGDEH SVSSSIVSEA CNKDGKSHRN AHDTTMAFKR KERIKDKSRA SEDPLVYLLQ
SAVTIQDNLE AEKMTYLTYN PEYISNSKVE NTVNHCKHLL HEQEMDPCTV SNSNKAVISC
STLGNDTSFS ISCQTPSCAS VCDEKLTASA ECAHQPRQER KEVGRDDERR EMMGRVSPNT
MNNIEFMCTD QDLTGESINR ETDVLLGKEL VKLSKRSLEY QQMHTDCNLS KTEEQYIGRD
RSVSLPATLS VPLDSNQSSY LKLECSDVNV PKGHCLSSSK NPGPGHTQPL KRRLSTPTNH
KNSNGKQLIC SNADSLEYLN AYPTFNQSNS VFPDIKVIST ENEIERTKSK VEYQAHAQYV
GSPSLSTNPN SNQNRPPITK ESPSVFRSNA SCIFQEVPSK AKQSDQVMTE NKEIMRFSSS
DINPFVHSWQ LDGSGKGRLK QCVFNSTSDV SCSKFQEQIM RCSSVDEGLN AHVSPFHSHL
SSYANAKMAS STISSTEDVQ IRNNTTQDFQ STNSLDGSSY YYPLSDEVAA LSYDCGPQHN
RSYELKPKSE NCSVQVDEIM VLYTSESETC NDDNIKVKSE QGTQTKGRYR RLNRHQRSHT
DVSSIKVTQC RNHRPASWSN MQNMSLHLSQ LLYETSELLG NFSEHDSGHM HFHTNSTEKA
VNKATRDSST QTTVDRGIQT DCQVSICTQN KDNEKEKLGS NIIVTSSQTQ HQRNQEKQIA
HDASIAKTQS LPNLHDGCSC EQRGPLYSST HFRTSTPFLA HVPSGISPSS YATRPSSFSP
FSENSPSEGS CTEVGGSECS TTRKLYNVEH NATEKLSERS NIGEGTVMVD RATSPILTLK
ASKKSLHKHT VAPTLNSQNM VKVLRHRSPK ERGSSQTVSD SENASSQSGS ENANPFRMPC
GSQFKDSARK RLKEEYMQPY RFKSEDCIVR EEHPFHRNRS SSISELSSIG RPSRDYNLFA
LKRRDKADGT SATALNAQHP LGRSPSLENL SPVKHQAPNR IVQRKRYSMV DNGFGSNSMT
SSNLLLKDKS HTISISEASN VQEDELSVVE SESNTDILLN TDSPIGMSRK SHNYTLQDLP
IHNKFSNWSG VQCTPSRLLP GSPAQLSLRD SPTKTEYSMQ KEEQEHSAST VCESRTQEIE
RLQRERAEIM SGIHLELNLQ PLTVQLAEAK LSYGIGETDA LLRVMQNGTT DDKKDIMSLK
KQLYDRHMKE IEGLRKERED RLQIFRRSRS LSPQKQLSAS QGSLASLRES DLPSRRREYL
QQLRKDVVDH TRFQEPKKGP TQCPSEIELM LKDYQKAREE AKSEIARARD KLRERAELER
KRLQQSCLIK EDTKLKSLMS TSTLCTSSNL SLSSGPTSGY NSSVTATQDK RSHQDLNETK
TSPRKMDLAS GVARGRSAVR NCQLVTSSQR EPVPDVRSQS QTPAEGKAPG DLPPATSHSS
YTPFISGLSH SVVSYQDIAR QLQTSAIAEI MAASFSNIKN LFDYQAAAGW IYQCTERDVL
VYYKAFPSAT KHGFLGAGVI RRPLHDVWGI VKDTDTRHLY DNSILTAQVH QRVANNIQLV
YVRSDASLCY LKQPRDFCCI TVESKEDAGY NLCFQSVYSE SMPRPSSDTV RGELLPSAWM
LQPDTINGEN VTRVIYLLQV DFGAPAVPSR LLKAISKRQP LVIASLASFL SV
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