ID A0A452FKD1_CAPHI Unreviewed; 4605 AA.
AC A0A452FKD1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Dynein axonemal heavy chain 14 {ECO:0000313|Ensembl:ENSCHIP00000024738.1};
GN Name=DNAH14 {ECO:0000313|Ensembl:ENSCHIP00000024738.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000024738.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000024738.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000024738.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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DR EMBL; LWLT01000016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9925.ENSCHIP00000024738; -.
DR Ensembl; ENSCHIT00000032599.1; ENSCHIP00000024738.1; ENSCHIG00000021801.1.
DR GeneTree; ENSGT00940000160505; -.
DR OMA; MFYNDCI; -.
DR Proteomes; UP000291000; Chromosome 16.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 1.10.287.2620; -; 1.
DR Gene3D; 1.10.8.1220; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.1270.280; -; 1.
DR Gene3D; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.920.20; -; 1.
DR Gene3D; 1.20.920.30; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 6.10.140.1060; -; 1.
DR Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 6.
DR Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR041658; AAA_lid_11.
DR InterPro; IPR042219; AAA_lid_11_sf.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR041589; DNAH3_AAA_lid_1.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
DR InterPro; IPR041228; Dynein_C.
DR InterPro; IPR043160; Dynein_C_barrel.
DR InterPro; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10676:SF356; DYNEIN AXONEMAL HEAVY CHAIN 14; 1.
DR PANTHER; PTHR10676; DYNEIN HEAVY CHAIN FAMILY PROTEIN; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12775; AAA_7; 2.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Dynein {ECO:0000256|ARBA:ARBA00023017};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT DOMAIN 984..1385
FT /note="Dynein heavy chain linker"
FT /evidence="ECO:0000259|Pfam:PF08393"
FT DOMAIN 1520..1853
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT DOMAIN 2082..2267
FT /note="Dynein heavy chain AAA 5 extension"
FT /evidence="ECO:0000259|Pfam:PF17852"
FT DOMAIN 2571..2659
FT /note="Dynein heavy chain 3 AAA+ lid"
FT /evidence="ECO:0000259|Pfam:PF17857"
FT DOMAIN 2720..2979
FT /note="Dynein heavy chain AAA module D4"
FT /evidence="ECO:0000259|Pfam:PF12780"
FT DOMAIN 2993..3323
FT /note="Dynein heavy chain coiled coil stalk"
FT /evidence="ECO:0000259|Pfam:PF12777"
FT DOMAIN 3352..3572
FT /note="Dynein heavy chain ATP-binding dynein motor region"
FT /evidence="ECO:0000259|Pfam:PF12781"
FT DOMAIN 3906..4022
FT /note="Dynein heavy chain region D6 P-loop"
FT /evidence="ECO:0000259|Pfam:PF03028"
FT DOMAIN 4060..4196
FT /note="Dynein heavy chain AAA lid"
FT /evidence="ECO:0000259|Pfam:PF18198"
FT DOMAIN 4204..4600
FT /note="Dynein heavy chain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18199"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 337..364
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3208..3291
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4605 AA; 530896 MW; D11B55FA6459DC15 CRC64;
METFRPNDLT PVNKDRNKDK GNSKPRVLKH EEENYFQDIL PSGNRPAGKE TLKHKTFGTI
SVPWKSEKVE EIYQDYTPDY LQAIRIQQDI LTSEPLPSKK KEKSKEKDQT HGCPKVRKKR
LASYDRTVPN DDDVICHIIR LREKLGWQTV LPQHSLEYRC FKTATQKILL KEPLKDDGEF
VYCLLRKNSK AFYNPYDLYV VSAHRARHCK EFWIITASFI SKVTKIGGKE EIELIPTLEW
LLERRCYYLL QQFKIFSNFR INKLFVTWKL TVKRIKTDKS RSLLYRNLFF ADELFQGCLL
YIKGLCEDAV SLKKGDEDNS NAICLVKLDK FRTYSLHEFC EEQLHQATQA LKQLEDIRDK
AISEIKLTIL KVAEKKDIKE YFESNHFEDT THFKLPTYRR LLEVIFRFLM LVDYLFQELT
RQLMNTAVTL LVELFSDSAR MPVSVEKKNE KLINIHKDIF AFTGKMTSDY EEFDNSNLYA
YSVLKSEVKT QDNEILNSIK VDTDLRKIHA PIFEVSLQLR TPAESDSSEN SEENLHESDK
CSEKSAVYED TSENEVSVFI EQSSEELLPM KKSKRMSYSY DVLSELDFET EFEKNCMNDK
LFEFPTNLFI TPNRLEFSVQ IQNMVAAFEN CITKIIPLCQ DPRLSMFTES ALIMDLPNKK
KNVRDYQTRW PDCQVLFEMD PAYQDKIATF LTIIGSSMGQ VSIYSCQFRK YCTMVEKAKI
IGTKISSMEE LTSTQFKSIL SKFRNYLRQI VNMTIEKRIG IFNVMSFDYQ LQCLPYVENI
IDMSQNLLRS AIERKNANLL EVIESSLQKL EYTPTEMEEF LEYFTFLDAI SSKISKLEKE
YIIVAQLYSV VRYYQIHVSE EQTAIYKILL IKFGQLKTSV KLSEKNKDAA ISKFRDNLES
YITDLCIEVS NLKAKIRNSV LLCASTPVST AMEMIQTLSE EAASLAVKAK TYSNYQDCFD
DSPSHMYFLN TEEITQIVLS EIADIDYDLT LRKILWDAEE EWGTLFWEWR NSTLDSIDTE
SVYRNVSKWM QIIFVLEKGL PKNDMVTHLK QSVIDFKQEL PIIIALGNPC LKPRHWEALQ
EIIGKSVSLD KNCTVENLLA LKMFQYENEI NEISTSATNE AALEKMLYKI IDLWNTTPLH
LVLHHTEAYS ILIISSIDDI LVQLEESQII LASVKGSSYL GPIKDLVDEW DQNLALFSYT
LEEWMSCQRN WLYLEPIFLS TEIQRQLPAE AKLFSQVISM WKEIMLKIHN KLDALQIATS
AGVLEILQNC NIHLEYIKKN LEDYLETKRM IFPRFYFLSN AELLDILSDS RNPECVQPHL
VKCFENIRRL LIWKQEIGPP AVVMFISAEG ETLVLPKKIR IRSGIEQWLV NVEKTMFDLV
KKFVSQGVDD WYYQQFSLWV LSHPGQVVLT VSQIIFYNDC IKSFVSSHPK KEVEKVHAGM
IHQLEEIAEL VLLDTHNSRA KVVLGALLTL YVHCRDTVRD LLLKSIFNAD DFEWTRHLQY
KWNEKQKLCY VSQGDASFTY GYEYLGCTPR LVITPLTDRC WLTLTGALHL NLGGCPAGPA
GTGKTESVKD LAKSLGKHCV VFNCFEDLDY KIMGKFFFGL VESGAWCCFD EFNRIDVEVL
SVIASQMLTI KAAKDSYSVR FILEGKEIRI NMSCAVFVTL NPGYKGRVEL PDNLKSLFRP
VAMMAPHYQM IAEIMLLSIG FKSAKLLSGK LVNIYELASK QLSHQDHYDF GLRSLKTVLV
MAGKKKRELK CNISDISETE ETLIIIEAMR EASLPKFLPK DVLLFEKIMR DIFCGATVSK
VNQIVLEKLI EIATQQLGLQ QWPAQKERII QFYNQLQACV GVMLVGPTGG GKTTVRRILE
KALTLLPIEE FLSIEERDSI SQVSGRRGKI DICILNPKCI TLSELYGHLD PNTMEWADGL
LSATIRNYVY LNTTKYSNKD NESKISDSAN VFKLDFSDAA DSDYHIFDKE MEKDIKIPES
QNFDWQWIVL DGPVDSFWVE NLNSMLDDTR TLCLANSERI TLTSKIRVIF EVDSLAQASP
AIVSRCAMVY MNPIDLGWEP YVKSWLLKNS KIMNEAEVDC LEFMIKSSVP DGLQFIKKHQ
KFQPFPVQDI TIVTTLCRIL DAFFEFMSKT GIFELREDLK DISSEEIISH SKVSVKFKDV
ENRDENAWYM AKNPIKLKKT IQKLFVFAFT WAFGGTLQRE DEHEDDIIFY PSSEPDSPAR
VAYDFDNLVR ELFEGNAQIG INLPNGEHSI FGYFVDIQQC EFIPWSELLP NVQTLVQRGT
SILTDPQGSS ENLLKITECG ESINYIATRD TTCLSFLVSL LLKNSCPVLL TGDFGVGKTA
AINQMLEKLE GSGAFDVKYG SILGEVLLYN EIKKSSFKQN ISILLSETHK TATGGLDKIT
KKAEVKTDES SFKNSNKGII VSAINFNINT SAARTKEMIL KKLVRRTKDS LGAPKNNRIV
IFIDDLNMPE SDMYGTQPPL ELIRQLLDMG GIYDTEKVTW KNIQDLSLVA ACVFPVSRRY
ISPRLLKHFS ILVLPHLPQT AIKTIFQVHL GMYFSINNFA PEVQKTKDQI ISCCLAVYYQ
VCQTMLPTPT KCHYMFNLRD VFKLLLGLLQ ADKYVVNSKE MAALFFVHEA TRVFHDRLLE
QAEQVLFYQI LSKELENYFQ IQWTKEKLMN DPIIFVDFLD VNKSHKKKTY QYTNDYNKLA
EVLTEFQMKL NSASLEISHS LVFFKEAIEH IARATRILRQ SGSHMLLIGI DGCGKETCAT
LACYLAEHKI FRVPLSHNYA YLEFKEDFKK VFMQAGLEGN PSALIVSNLN LDQELFMEDL
NSIINLGKIP DLFENEELDA IALRLRSLAE QSGYVDNRQA LLSFFQKRIH KNLHILMTMS
PTRPNFHQNC RLYPSLISSC TVDWYEKWPE EALLIVADAF LREKVDIKNR ENLKEKLVPT
CVQIHQSVKE LNIKYFQTTR RHYYITPSNY LRFMDTFAHI LKSREKEMQK KRERFHMGLS
KILETTALVT DMQEELLILG PQIEQKTKEK EILMEKLQKD SQVVEKVQML VKQDEEIMEE
EVRIVEEYAQ KADNELKSVL PALDKAIVAL NALDKADVSE LRVYTRPPYL VLTVMNAVCI
LLQKKPNWAT AKLLLSETGF LKKLINIDKD SIPEKVFIKL KKILVLPDFN PNKIALVSVA
CCSMCQWVIA LNSYHEAQKL VGPKQIQVAE AQNVLKIAKQ RLDEKQRGLQ LVEEHLQFLQ
EAYKEIVAEK ELLAHRRKLA TKRLQCASIL LTALEDEKTR WQETIDQIDN KLEGILGDIL
ISAACIVYSG VLTAEFRQLI VEKWQNLCTE NNISLSSNFS LIEVMAQKHE IRQWHHQGLP
LGQYSTENAI LIKNGLQWPL LIDPQKQAHS WIRQMEGSRL QELSTEDSNY IQTIENAMKT
GGSVLLQNLP ERLPPSLKEI LKKDIYQRRG QYFIKINDSE IEYNSKFRLY VSTEIDNPYF
PPFIYSFVTM INFTVTFQGF QDQLLSIVLS HEVPHLENQR FQLLESISLD AKTLEELEQK
TLNLLENAQG FVLDDEEIVD ILRKSKMTSN EISKRIKATR KAESKIEETR KVYLPIATRG
ALLYFLVSNL AQIDYMYQFS LDWFRQIFVS SVVSKSKEQE EHSLKRETMF LQKGHEIPNL
SKEPKLGSEK RTLDRHLKNS IDTLTRNIFK VVSLALFNRH KLCFSFGLCT TIMQNNANGN
LMQDDIGSLP KEEWNIFLNS STLVNIKGVM PQPKLNSIYE TCKNQHLQWV SDSRWKQCFY
ISNELEPFSL LCKSLLSNVS QWNAFKNSNT VYLLMSTAFS SENASMEESE KSPEIAQVFN
ENEEIYTSIN FPWEKLTPFQ RLILIKILRP EHLKNSVERF ITEKIGNEYI HSTGTSLKES
YEESNARTPL ILIHSHGIDL TNTLLKFAQE LMGTTNHVTM ISLGRGQAAK AEALIVKALT
NTEQWVFLQN CHLAASFMPR LCTIVESFNS PDVTIEPKFR LWLSSKSDSS FPIPILQKSL
KIAVENPQGL KNNLLQTFGY SGSGEVTEEL FEKPDCGPWW KKILFSLCFF NALINERKIY
GILGWNIAYA FSSSDLEVAI KVLENFLSAQ SSIPWQTLRY LIGEVVYGGW VTDTWDRRCL
NTLLYKFCNP EVLKDDFSFS TDEPLPKSGS MKDYIHAIQS LPDDDPPELL ELHPEATRGF
REIQAQKFID NLIGMQPRFT ITNLIFSREK SKDELVMAML SDMLTRLPLS VEKEEWAGTP
STLKYIMLSP IWESFHKDPK GYDPLIHCVL LTFLIQEIER FDQLLSIIHK SLKDLRLAIK
GEIILTQELE EIYDSFLNTK VPKLWQKYAY KSSKALSSWV NDLIQRLNFF NTWAKMAYTA
MHHRYMRLVT AWKHSSTSPS QDPKYPTEQN SEFFEGFPAR YWLPAFFFPQ AFLITVLQDY
GRSQGISTDA LTFTHHVISD TTDVKDKEFS IIIQKKLNIV RRAFKGTDPT HVGVHVFGLF
IEGARWNHKE KILEDSLPCE ICCDFPEIYF LPTKISSESS TASKQTEPEL YTFECPVYQT
PERSSILTAA GLSSNFLTSV YLSTKKPPSH WITMQVALLC EENEK
//
