ID A0A5N5LW44_PANHP Unreviewed; 3964 AA.
AC A0A5N5LW44;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE RecName: Full=Dynein axonemal heavy chain 12 {ECO:0000256|ARBA:ARBA00069442};
GN ORFNames=PHYPO_G00070740 {ECO:0000313|EMBL:KAB5546326.1};
OS Pangasianodon hypophthalmus (Striped catfish) (Helicophagus hypophthalmus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Pangasiidae; Pangasianodon.
OX NCBI_TaxID=310915 {ECO:0000313|EMBL:KAB5546326.1, ECO:0000313|Proteomes:UP000327468};
RN [1] {ECO:0000313|EMBL:KAB5546326.1, ECO:0000313|Proteomes:UP000327468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indonesia {ECO:0000313|EMBL:KAB5546326.1,
RC ECO:0000313|Proteomes:UP000327468};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB5546326.1};
RA Wen M., Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Avarre J.-C., Campet M., Ha T.T.T., Dugue R., Lampietro C., Louis A.,
RA Herpin A., Echchiki A., Berthelot C., Parey E., Roest-Crollius H.,
RA Braasch I., Postlethwait J., Bobe J., Montfort J., Bouchez O., Begum T.,
RA Schartl M., Guiguen Y.;
RT "A chromosome-scale genome assembly of the striped catfish, Pangasianodon
RT hypophthalmus.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Force generating protein of respiratory cilia. Produces force
CC towards the minus ends of microtubules. Dynein has ATPase activity; the
CC force-producing power stroke is thought to occur on release of ADP.
CC Involved in sperm motility; implicated in sperm flagellar assembly.
CC {ECO:0000256|ARBA:ARBA00057074}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains. {ECO:0000256|ARBA:ARBA00011655}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000256|ARBA:ARBA00004230}. Cytoplasm, cytoskeleton, cilium
CC axoneme {ECO:0000256|ARBA:ARBA00004430}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB5546326.1}.
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DR EMBL; VFJC01000017; KAB5546326.1; -; Genomic_DNA.
DR Proteomes; UP000327468; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 CDD; cd00009; AAA; 1.
DR FunFam; 1.20.920.30:FF:000002; Dynein axonemal heavy chain 3; 1.
DR FunFam; 1.10.8.1220:FF:000001; Dynein axonemal heavy chain 5; 1.
DR FunFam; 1.10.8.710:FF:000004; Dynein axonemal heavy chain 6; 1.
DR FunFam; 1.20.140.100:FF:000004; Dynein axonemal heavy chain 6; 1.
DR FunFam; 3.40.50.300:FF:002141; Dynein heavy chain; 1.
DR FunFam; 1.10.472.130:FF:000011; dynein heavy chain 12, axonemal; 1.
DR FunFam; 3.20.180.20:FF:000003; Dynein heavy chain 12, axonemal; 1.
DR FunFam; 3.40.50.300:FF:001112; Dynein heavy chain 12, axonemal; 1.
DR FunFam; 1.10.287.2620:FF:000002; Dynein heavy chain 2, axonemal; 1.
DR FunFam; 3.40.50.300:FF:000223; Dynein heavy chain 3, axonemal; 1.
DR FunFam; 3.40.50.300:FF:000044; Dynein heavy chain 5, axonemal; 1.
DR FunFam; 1.10.8.720:FF:000001; dynein heavy chain 7, axonemal; 1.
DR FunFam; 1.20.1270.280:FF:000001; dynein heavy chain 7, axonemal; 1.
DR FunFam; 3.10.490.20:FF:000001; dynein heavy chain 7, axonemal; 1.
DR FunFam; 1.20.58.1120:FF:000005; Dynein, axonemal, heavy chain 12; 1.
DR FunFam; 1.20.920.20:FF:000006; Dynein, axonemal, heavy chain 6; 1.
DR FunFam; 3.40.50.300:FF:000362; Dynein, axonemal, heavy chain 6; 1.
DR FunFam; 3.40.50.300:FF:005585; Predicted protein; 1.
DR Gene3D; 1.10.287.2620; -; 1.
DR Gene3D; 1.10.472.130; -; 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; 5.
DR Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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.
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; PTHR22878:SF70; DYNEIN HEAVY CHAIN 2, AXONEMAL; 1.
DR PANTHER; PTHR22878; DYNEIN HEAVY CHAIN 6, AXONEMAL-LIKE-RELATED; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12775; AAA_7; 1.
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 SMART; SM00382; AAA; 3.
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 Flagellum {ECO:0000256|ARBA:ARBA00022846};
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:UP000327468};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 1271..1410
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1552..1691
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1906..2054
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 19..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 639..666
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2760..2815
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 29..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3964 AA; 453049 MW; 052E843F060B07CC CRC64;
MPTSSAACKA SLEDGLRKYT VLPPIPSPPE RENSSLPEHR AAVRRKLLCY SRSKQQQHEL
HKIMVASATQ AYIKAKDTMD SPYSEPEFPS AMMSEARKQQ MNYMFLKQCV ESRPIVPIQQ
QWLDNMLSLI PPQLRLEPGR TELLEELCKE VSTNFLSTMV KFTVNNILQK PQMDTDVPLQ
KPPAPKILDF SRPWHKSFIR SRKKIKENLH ILHPVMKVIL DTCYITFSQL LLVDISDCRS
TGPVDCENLK NKVSLECEKI EEKLMNTWFP KVIHLLTSKN TVQRIRGEKL DAFYNCASTL
LSNQLKALIE RNVEAYVSLF EPLNKEKLPL FRMDLTFDDE KMDFYPSFQD LEEAVLEIFN
SIINTLQKVQ TVQSWLDEAN SSVVDAKLAD HIVIWAQTTL RNAVRENLEA PAKHFQYYID
NYDWLVNGSA KNLVEKFMEE EHSFEQYTEQ VEVFRALSKE ISSLPSVAHF DMIRLDCEEL
KQGLAKKAQN FAQILVARLI STNRDQCLQI CKEFETIRDK VTKDPETTED MTEMIAYIDH
AKTKGIEELS SKIMETHRRL NYLLDVHIFD AEDLELHSTV LLWPQNINPI FELSVEVLEK
AKQRGEQELL GRREKLMLEL VKLGRRTEEF SACSELDMMQ QYVIDVRTVQ KRLQEVEESI
VFINKEEALY NWDLTVYPEV DMIKENIEPY QKLFGLVLKW QRTEKRWMDG SFLDLNGESM
EVEVDEFFRE IYKSLKFFQQ KQKKAEQERA SVAAEKRRPG EEDEDKEESS TAAVCCRVLE
QIKEFKEHIP TVSILCNPGI RVRHWEQMSE IVNFDMMPNS GTTLRKVLKQ NLTSYMEQFE
TISAAAGKEF SLEKAMQNMV EGWDAVSFHH HAYRESGVSI LTAVDEIQTM LDDQIVKTQT
MRGSPFIKPF EAEIKAWEER LIHIQDTIDE WLKVQAQWLY LEPIFSSQDI MQQMPEEGRL
FQMVDKHWKE VMRHCVKDSK VLPATSLPGL LEKLQDSNNL LDQIMKGLNA YLEKKRLFFP
RFFFLSNDEM LEILSETKDP LRVQPHLKKC FEGIAKLDFM PNLDIQAMYS SEGERVGLIQ
LISTSEARGA VEKWLVQVED MMLRSIRDVI NRARLAYPES KRSQWVCDWP GQVVLCTSQI
YWTLEVHEAI RSGINGLKDY YDQLQNQLND IVELVRGKLP KQTRTTLGAL VTIDVHARDV
VMEMIQKGVS CETDFQWLAQ LRYYWTNENV RVCIINCDVK YAYEYLGNSP RLVITPLTDR
CYRTLIGAFY LNLGGAPEGP AGTGKTETTK DLAKALAVQC VVFNCSDGLD YLAMGKFFKG
LASSGAWACF DEFNRIELEV LSVVAQQILC IQRAIELKLE VFDFEGTELR LNPNCFVAIT
MNPGYAGRSE LPDNLKVLFR TVAMMVPNYA LIAEISLYSY GFLNAKPLSV KIVMTYRLCS
EQLSSQFHYD YGMRAVKAVL VAAGNLKLKF PNENEDILLL RSIKDVNEPK FLSHDIPLFN
GITSDLFPGV SLPTADYQLL LACAHECCIK HNVQPVNIFL DKIIQTYEMM IVRHGFMLVG
EPFAGKTKVL HVLADTLTLM NERGYNEEEK VQYLTVNPKS ITMGQLFGQF DPVSHEWTDG
IVANTFREFA SAETPDRKWV VFDGPIDTLW IESMNTVLDD NKKLCLMSGE IIQMSNQMSL
IFEAMDLSQA SPATVSRCGM IYMEPSQLGW PPLVSSWLKT LPQPLQTQEN STLLLELFNW
LIPPAHRMLR KNCKEVVSTS NSNTVVSLTR LFEMLLTEPV NEEPGNKNIR TWIMAAFAFS
LVWSVGGSCD GDSRERFDKF LREIIMGKSD NHPIPDTVSK WECPFDEKGL VYDYSYEFKG
KGHWIHWNES IKNVTLGDKN TKVQNIIVPT IDTVRYTYLM DLCINYGMPL LFVGPTGTGK
SVYVKEKLMN NLDKDRYLPF FINFSARTSA NQTQNIIMSR LDKRRKGVFG PPMGKKCIIF
VDDMNMPAME VFGAQPPIEL LRQYFDHGNW YDLKDTSKIT LVDLQLIAAM GPPGGGRNAV
TSRFLRHFNI CSINAFSDDT MSRIFSNVVA FYFRNNGFPP DCFTIGNQIV SATLEVYKKA
MQNLLPTPAK SHYTFNLRDF SRVVQGCLLL KKESLESKHT LIRLFVHEVF RVFYDRLVDE
QDQAWLYKLM NVIVKEHFKE NFDTVFEHLK SDKKSLCEEN MKSLLFGDYM NPDVDPSERL
YAEVPSMESF SQVVESCLAE YNQTHKNRMN LVIFRYVLEH LSRISRVLKQ PGGNALLVGV
GGSGRQSITK LATFMAGMTL FQPEISKNYG MNEWRDDLKL LLKNAGVKGQ KTVFLLTDAQ
IKEEAFLEDV DSVLNTGEVP NIFAVDEKQE IMEAVRPIAQ AGNKNLEFSP LALFAYFVNR
CRENLHIVVA FSPIGDTFRN RLRQFPSLIN CCTINWFQPW PEEALERVAT KFLETLEMND
HERLEVMLIC KTFHTSATDL SKRFLSELGR HNYVTPTSYL ELIAAFRLLL TQKRDTVMKA
KKRYTNGLDK LAFAESQVGE MKKELVDLQP KLEQAKIDNT NIMKVIEVES VQVEAKSKVV
RVDEEAATQK ANEAQALKNE CESDLAEAIP ALEAALSALD TLKPSDITIV KSMKNPPAGV
KLVMAAVCVM KDIKPEKIND PAGTGKKIED YWGPSKKLLG DMNFLRDLKE YDKDNIPAQV
MHKIRSEYMT NPDFDPTKVV KASSAAEGLC KWITAMEVYD RVAKVVAPKK ANLAVAQESL
AATMALLNQK RAELKEVEDR LASLQKTFEE KTEEKAQLEF QVDLCARKLE RAEKLIGGLG
GEKTRWSKAA DDLQNTYDNL TGDVLISAGV IAYLGAFTAG FRQDCIKDWT KLCKSKKIPS
SDDFSLSKTL GDPIKIRAWN ISGLPTDSFS IDNGVIVSNS RRWPLMIDPQ GQANKWVKNS
ERENNLNVIK LTDADYMRTL ENCIQFGTPL LLENVGEELD PSIEPLLLKQ IFKQGGMDCI
RLGESVIEYS SEFRFYITTK LRNPHYLPEL ATKVSLLNFM ITPEGLEDQL LGIVVAKERP
ELEEERNALI LQSAANKKQL KEIEDKILET LQSSEGNILE DESAIQILDS AKIMSNEISK
KQQIAEKTEI KIAESREGYR AIAKHSSILF FSIADLANID PMYQYSLSWF VNLYINSIQD
SNKSKILEKR LRYLNGHFTY NLYCNVCRSL FEKDKLLFSF LLCCNLLLAK KEIMYSDFMF
LLTGGVGLQN DVPNPDPSWL QEKSWDEICR ASELPGLQGL RESVIKAPES FLPIYDSKEP
FNTPLPSPWC DKLNDFQKMI IYRCLRPDKI EPAITNYVTD KLGKKFVEPP PFDLSRSYVD
SNSTIPLVFV LSPGADPMAS LLKFANDKNM GGTKFKSISL GQGQGPIAVK MIQSAMKEGT
WVCLQNCHLA VSWMSTLEKI CEDFSPDTCH PDFRLWLTSY PSPMFPVTIL QNGVKMTNEP
PTGLRLNLLQ SYLSDPISDP EFFSACPGKE PVWEKLLYGV CFFHALVQER KKFGPLGWNI
PYGFNESDLR ISIRQLQLFV NEYEEVPFEA ITYLTGECNY GGRVTDDWDR RLLLTILADF
YNKDIIKNPR YNFSPSGKYY APPKSIYEDY VDFIRSLPST QHPEVFGMHE NVDISKDLQQ
TKLLFDSLIL TQGGGSKGGG SSEGDNNLLD IASDILYKLP ENFNIEAALA KFPVQYEESM
NTVLVQEMER YNNLCKTICV SLQNLLKAIK GLVVMDAELE AIASSLLVGK VPEKWAKRSY
PSLKPLGSYI TDLLARLKFL QDWYDTTKPH VFWLSGFFFT QAFLTGAMQN YARKYSIPID
LLVFDYEVMP FDTSDTSPDD GVYTHGLFLD GARWDKKSGV LAEQYPKILF DSVPIIWIKP
TDKRVMTQPQ NIYVCPLYKT SERKGTLSTT GHSTNFVISM MLPTSKRPQH WIKRGVAMLC
QLDN
//
