DYH7_HUMAN
ID DYH7_HUMAN Reviewed; 4024 AA.
AC Q8WXX0; B8ZZX8; O00433; O95492; Q4G152; Q53QX7; Q53S64; Q53T02; Q68CY5;
AC Q8N1Z2; Q9UMS3; Q9Y2F3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Dynein axonemal heavy chain 7;
DE AltName: Full=Axonemal beta dynein heavy chain 7;
DE AltName: Full=Ciliary dynein heavy chain 7;
DE AltName: Full=Dynein heavy chain-like protein 2;
DE AltName: Full=hDHC2;
GN Name=DNAH7; Synonyms=KIAA0944;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, AND
RP VARIANT PRO-3319.
RC TISSUE=Tracheobronchial epithelium;
RX PubMed=11877439; DOI=10.1074/jbc.m200348200;
RA Zhang Y.J., O'Neal W.K., Randell S.H., Blackburn K., Moyer M.B.,
RA Boucher R.C., Ostrowski L.E.;
RT "Identification of dynein heavy chain 7 as an inner arm component of human
RT cilia that is synthesized but not assembled in a case of primary ciliary
RT dyskinesia.";
RL J. Biol. Chem. 277:17906-17915(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS CYS-545
RP AND PRO-3319.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP SEQUENCE REVISION.
RA Nagase T., Kikuno R., Yamakawa H., Ohara O.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1290-1432 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 1356-1422 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Nasal polyp;
RX PubMed=11175280; DOI=10.1038/sj.ejhg.5200555;
RA Maiti A.K., Mattei M.-G., Jorissen M., Volz A., Zeigler A., Bouvagnet P.;
RT "Identification, tissue specific expression, and chromosomal localisation
RT of several human dynein heavy chain genes.";
RL Eur. J. Hum. Genet. 8:923-932(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1333-1503 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=9373155; DOI=10.1016/s0378-1119(97)00417-4;
RA Neesen J., Koehler M.R., Kirschner R., Steinlein C., Kreutzberger J.,
RA Engel W., Schmid M.;
RT "Identification of dynein heavy chain genes expressed in human and mouse
RT testis: chromosomal localization of an axonemal dynein gene.";
RL Gene 200:193-202(1997).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The dynein complex consists of at least two heavy chains and a
CC number of intermediate and light chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:11877439}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8WXX0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WXX0-2; Sequence=VSP_031131;
CC Name=3;
CC IsoId=Q8WXX0-3; Sequence=VSP_031132, VSP_031135, VSP_031136;
CC Name=4;
CC IsoId=Q8WXX0-4; Sequence=VSP_031133, VSP_031134;
CC -!- TISSUE SPECIFICITY: Detected in brain, testis and trachea. Detected in
CC bronchial cells (at protein level). {ECO:0000269|PubMed:11175280,
CC ECO:0000269|PubMed:11877439}.
CC -!- INDUCTION: Up-regulated during ciliogenesis (at protein level).
CC {ECO:0000269|PubMed:11877439}.
CC -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC (which binds cargo and interacts with other dynein components), and the
CC head or motor domain. The motor contains six tandemly-linked AAA
CC domains in the head, which form a ring. A stalk-like structure (formed
CC by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC and terminates in a microtubule-binding site. A seventh domain may also
CC contribute to this ring; it is not clear whether the N-terminus or the
CC C-terminus forms this extra domain. There are four well-conserved and
CC two non-conserved ATPase sites, one per AAA domain. Probably only one
CC of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC regulatory function (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76788.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB06055.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAH18445.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18445.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AF327442; AAL37427.1; -; mRNA.
DR EMBL; AB023161; BAA76788.2; ALT_INIT; mRNA.
DR EMBL; AK094515; BAC04372.1; -; mRNA.
DR EMBL; CR749651; CAH18445.1; ALT_SEQ; mRNA.
DR EMBL; AC013274; AAY14776.1; -; Genomic_DNA.
DR EMBL; AC068919; AAY14995.1; -; Genomic_DNA.
DR EMBL; AC104600; AAY24051.1; -; Genomic_DNA.
DR EMBL; AC114760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029567; AAH29567.1; -; mRNA.
DR EMBL; AJ132084; CAA10557.1; -; mRNA.
DR EMBL; AJ132093; CAB46444.1; -; Genomic_DNA.
DR EMBL; Z83801; CAB06055.1; ALT_FRAME; mRNA.
DR CCDS; CCDS42794.1; -. [Q8WXX0-1]
DR RefSeq; NP_061720.2; NM_018897.2. [Q8WXX0-1]
DR RefSeq; XP_011509789.1; XM_011511487.2.
DR PDB; 6RZA; EM; 5.40 A; X=2675-2812.
DR PDBsum; 6RZA; -.
DR SMR; Q8WXX0; -.
DR BioGRID; 121102; 9.
DR IntAct; Q8WXX0; 2.
DR MINT; Q8WXX0; -.
DR STRING; 9606.ENSP00000311273; -.
DR GlyGen; Q8WXX0; 1 site.
DR iPTMnet; Q8WXX0; -.
DR PhosphoSitePlus; Q8WXX0; -.
DR BioMuta; DNAH7; -.
DR DMDM; 311033375; -.
DR EPD; Q8WXX0; -.
DR jPOST; Q8WXX0; -.
DR MassIVE; Q8WXX0; -.
DR MaxQB; Q8WXX0; -.
DR PaxDb; Q8WXX0; -.
DR PeptideAtlas; Q8WXX0; -.
DR PRIDE; Q8WXX0; -.
DR ProteomicsDB; 75108; -. [Q8WXX0-1]
DR ProteomicsDB; 75109; -. [Q8WXX0-2]
DR ProteomicsDB; 75110; -. [Q8WXX0-3]
DR ProteomicsDB; 75111; -. [Q8WXX0-4]
DR ABCD; Q8WXX0; 1 sequenced antibody.
DR Antibodypedia; 49680; 44 antibodies from 13 providers.
DR Ensembl; ENST00000312428.11; ENSP00000311273.6; ENSG00000118997.14. [Q8WXX0-1]
DR Ensembl; ENST00000409063.5; ENSP00000386912.1; ENSG00000118997.14. [Q8WXX0-2]
DR Ensembl; ENST00000410072.5; ENSP00000386260.1; ENSG00000118997.14. [Q8WXX0-4]
DR GeneID; 56171; -.
DR KEGG; hsa:56171; -.
DR MANE-Select; ENST00000312428.11; ENSP00000311273.6; NM_018897.3; NP_061720.2.
DR UCSC; uc002uti.5; human. [Q8WXX0-1]
DR CTD; 56171; -.
DR DisGeNET; 56171; -.
DR GeneCards; DNAH7; -.
DR HGNC; HGNC:18661; DNAH7.
DR HPA; ENSG00000118997; Tissue enhanced (brain, choroid plexus).
DR MalaCards; DNAH7; -.
DR MIM; 610061; gene.
DR neXtProt; NX_Q8WXX0; -.
DR OpenTargets; ENSG00000118997; -.
DR PharmGKB; PA38625; -.
DR VEuPathDB; HostDB:ENSG00000118997; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000155282; -.
DR HOGENOM; CLU_000038_1_3_1; -.
DR InParanoid; Q8WXX0; -.
DR OMA; DKSMYTI; -.
DR OrthoDB; 2079at2759; -.
DR PhylomeDB; Q8WXX0; -.
DR TreeFam; TF316836; -.
DR PathwayCommons; Q8WXX0; -.
DR SignaLink; Q8WXX0; -.
DR BioGRID-ORCS; 56171; 7 hits in 1067 CRISPR screens.
DR ChiTaRS; DNAH7; human.
DR GenomeRNAi; 56171; -.
DR Pharos; Q8WXX0; Tbio.
DR PRO; PR:Q8WXX0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WXX0; protein.
DR Bgee; ENSG00000118997; Expressed in right uterine tube and 144 other tissues.
DR ExpressionAtlas; Q8WXX0; baseline and differential.
DR Genevisible; Q8WXX0; HS.
DR GO; GO:0005858; C:axonemal dynein complex; NAS:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0036156; C:inner dynein arm; IMP:SYSCILIA_CCNET.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; NAS:UniProtKB.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0003341; P:cilium movement; IMP:SYSCILIA_CCNET.
DR GO; GO:0060285; P:cilium-dependent cell motility; NAS:UniProtKB.
DR GO; GO:0036159; P:inner dynein arm assembly; IMP:SYSCILIA_CCNET.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.10.8.720; -; 1.
DR Gene3D; 1.20.140.100; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 3.20.180.20; -; 1.
DR Gene3D; 3.40.50.300; -; 5.
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; 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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF12774; AAA_6; 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; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell projection; Cilium;
KW Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..4024
FT /note="Dynein axonemal heavy chain 7"
FT /id="PRO_0000317666"
FT REGION 1..1289
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1511
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1571..1802
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 1938..2189
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2302..2555
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2572..2873
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 2954..3184
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3397..3620
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 685..745
FT /evidence="ECO:0000255"
FT COILED 2827..2883
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1328..1335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1609..1616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1976..1983
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2341..2348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..3517
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031131"
FT VAR_SEQ 1..1452
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031132"
FT VAR_SEQ 452..501
FT /note="ESKSKPTTLKPIILNEIVDAHKEKIKEVIMKESVAPTEHLRLYDKYDFLI
FT -> RNKAKPGHFYFSHIQRSVTFQHSEVSSPQNSHFKIVSPFSVLGFTWRCQL (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031133"
FT VAR_SEQ 502..4024
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031134"
FT VAR_SEQ 1633..1639
FT /note="GLMEENK -> ASILLMH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031135"
FT VAR_SEQ 1640..4024
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031136"
FT VARIANT 169
FT /note="H -> P (in dbSNP:rs1072599)"
FT /id="VAR_038580"
FT VARIANT 280
FT /note="A -> T (in dbSNP:rs2375643)"
FT /id="VAR_038581"
FT VARIANT 315
FT /note="I -> V (in dbSNP:rs17838596)"
FT /id="VAR_038582"
FT VARIANT 438
FT /note="S -> N (in dbSNP:rs16843720)"
FT /id="VAR_038583"
FT VARIANT 545
FT /note="R -> C (in dbSNP:rs10931715)"
FT /evidence="ECO:0000269|PubMed:10231032"
FT /id="VAR_038584"
FT VARIANT 565
FT /note="D -> H (in dbSNP:rs2635718)"
FT /id="VAR_038585"
FT VARIANT 675
FT /note="K -> E (in dbSNP:rs10198893)"
FT /id="VAR_038586"
FT VARIANT 825
FT /note="K -> E (in dbSNP:rs6719500)"
FT /id="VAR_038587"
FT VARIANT 1422
FT /note="P -> T (in dbSNP:rs168192)"
FT /id="VAR_038588"
FT VARIANT 1525
FT /note="E -> K (in dbSNP:rs13415574)"
FT /id="VAR_038589"
FT VARIANT 1886
FT /note="R -> Q (in dbSNP:rs13034775)"
FT /id="VAR_038590"
FT VARIANT 1940
FT /note="P -> L (in dbSNP:rs2375544)"
FT /id="VAR_038591"
FT VARIANT 1971
FT /note="P -> L (in dbSNP:rs2889109)"
FT /id="VAR_038592"
FT VARIANT 2020
FT /note="M -> T (in dbSNP:rs10184131)"
FT /id="VAR_038593"
FT VARIANT 2459
FT /note="N -> K (in dbSNP:rs16841199)"
FT /id="VAR_038594"
FT VARIANT 2569
FT /note="T -> I (in dbSNP:rs2293066)"
FT /id="VAR_038595"
FT VARIANT 2809
FT /note="I -> V (in dbSNP:rs16841018)"
FT /id="VAR_038596"
FT VARIANT 3319
FT /note="L -> P (in dbSNP:rs13411834)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:11877439"
FT /id="VAR_038597"
FT VARIANT 3386
FT /note="R -> H (in dbSNP:rs6708527)"
FT /id="VAR_038598"
FT CONFLICT 433
FT /note="M -> V (in Ref. 4; BAC04372)"
FT /evidence="ECO:0000305"
FT CONFLICT 1020
FT /note="I -> T (in Ref. 2; BAA76788)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292
FT /note="Y -> F (in Ref. 8; CAA10557)"
FT /evidence="ECO:0000305"
FT CONFLICT 1353
FT /note="N -> D (in Ref. 9; CAB06055)"
FT /evidence="ECO:0000305"
FT CONFLICT 1355
FT /note="S -> P (in Ref. 9; CAB06055)"
FT /evidence="ECO:0000305"
FT CONFLICT 1467
FT /note="Y -> H (in Ref. 5; CAH18445)"
FT /evidence="ECO:0000305"
FT CONFLICT 1502
FT /note="M -> L (in Ref. 9; CAB06055)"
FT /evidence="ECO:0000305"
FT CONFLICT 3563
FT /note="P -> L (in Ref. 7; AAH29567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4024 AA; 461159 MW; 3C2E3B2D7B886540 CRC64;
MSSEQDKSAS KEKSKKPVRF LPQLSMEKLA SKEKFKAPAR ALPQLSMVST KPHWQQAAPS
FHLSVKQDDE SPEPFSVKNE QSHAEYMERF GKKGKLPHQV DDSYVGPSTS KSKGKSPHKE
RENFRSTLVN VIMQQDADLD SAVPDGSTIP KPTASAIEKD ILRYYYYIHH GIDTDHVAPM
EDSWLEHVLD LVPQHLKVFT DSIVTLSDEM REDYLLSVRK SIVDFVLKDP REKGDDKKTD
ELPAHRAEME ILPKPWRKSF LAASSYIRDH LNAMNPTMLA VLDLWHTNFK KLRLVDIKEF
HNCQDALELS SFQNIIMRHM DSAKETLLKM WFPEVQNIYY QGNKKKQLPT GDSSAKLESF
FNCAAALMTL QLQDLTLVSM QDFTDLIAQP PDSVRAFEHP GFIMRLILDN DTIKFEPELS
DYIDIFLNVY DVMIKAVSFV PRVETKLYSK WESKSKPTTL KPIILNEIVD AHKEKIKEVI
MKESVAPTEH LRLYDKYDFL ITRKAERDVD NFLAENHSYE KIIDEICKYQ KLIEEIQYTS
IKTIRLGMFE MHCEELIRAL VKRADIICGK LLAKMFRDHQ EVNTRLCDEF ERIAEKALST
PPNTAELMEM KAYIQKVEVT DMIELEQRLV DSKNCLAFLI EYVNFSPADM RLNNSVFQWY
GRMGEIFEEH RKIIKEKIEQ YQEGLKLRCE RFVEELESYA KQSEEFYSFG DLQDVQRYLK
KAQILNGKLD LAADKIEQFN AEEEAFGWLP SVYPQRKKIQ DGLNPYLRLY ETAVEFSSNY
RAWTEGPYHK VNPDQVEADI GNYWRGLYKL EKTFHDSPYA LAMTKKVRSK VEDFKQHIPL
IQVICNPGLR PRHWEAMSAI VGYPLQPSDD STVSSFLDMN LEPYIDRFEG ISEAASKEYS
LEKAMEKMIT EWDAVEFVIH SYRETGTFIL ASVDEIQMLL DDHIIKTQTM RGSPFIKPYE
KQMREWEGKL LLLQEILDEW LKVQATWLYL EPIFSSPDIM SQMPEEGRRF TAVDKTWRDI
MRSVMQDKHV LTVVTIDRML ERLKKSNELL ELILKGLNEY LEKKRLFFPR FFFLSNDELL
EILSETKDPT RVQPHLKKCF EGIAKVEFTE TLDITHMKSS EGEVVELIEI ISTAKARGQV
EKWLVELERV MINSIHKVTG DATFAYTKYE RINWVRDWPG QTVLCVSQIF WTKEVQTAIP
MGIKALEQYL KTCNRQIDDI VTLVRGKLSM QNRVTLGALV VLDVHARDVL SSLVKKNISD
DSDFEWLSQL RYYWQENHLE TKMINAGLRY GYEYLGNSPR LVITPLTDRC YRTLFGALHL
HLGGAPEGPA GTGKTETTKD LAKAVAKQCV VFNCSDGLDY LALGKFFKGL LSCGAWACFD
EFNRIDLEVL SVVAQQILTI QRGINAGADI LMFEGTELKL DPTCAVFITM NPGYAGRSEL
PDNLKALFRT VAMMVPDYAM IAEIVLYSCG FVTARPLSVK IVATYRLCSE QLSSQHHYDY
GMRAVKSVLT AAGNLKLKYP NENEEILLLR SIIDVNLPKF LSHDLPLFEG ITSDLFPGVK
LPKPDYNDLL AAIKDNCASM NLQMTAFFSE KILQVYEMMI VRHGFMIVGE PFGGKTSAYR
VLAGALNDIC EKGLMEENKV QITVLNPKSV TMGQLYGQFD SVSHEWSDGV LAVSFRAFAS
SVTPDRKWLI FDGPVDAVWI ENMNTVLDDN KKLCLMSGEI IQMSPQMNLI FEPMDLEVAS
PATVSRCGMI YMEPHMLGWR PLMLSWVNLL PASVSVIQKE FIMGLFDRMV PVSVEFIRKH
TKELSPTSDT NLVRSLMNLI DCFMDDFADE VKLKERNDRE TYSLLEGIFL FSLIWSVGAS
CTDDDRLKFN KILRELMESP ISDRTRNTFK LQSGTEQTSS KALTVPFPEK GTIYDYQFVT
EGIGKWEPWI KKLKEAPPIP KDVMFNEIIV PTLDTIRYSA LMELLTTHQK PSIFVGPTGT
GKSVYITNFL LNQLNKEIYK PLLINFSAQT TAAQTQNIVM SKLDKRRKGV FGPPLGKRMV
VFVDDVNMPA REVYGAQPPI ELLRQWLDHW NWYDLKDCSM IKLVDIQIMC AMGPPGGGRN
PVTPRYMRHF NIITINEFSD KSMYTIFSRI LTWHLEICYK FPDEFLDLTT QIVNGTMTLY
KEAMKNLLPT PAKSHYLFNL RDFSRVIQGV CLSRPETTET TEVIKRLWVH EVLRVYYDRL
LDNTDRSWLI NYIQEILRNY MYEDFHELFQ RLDFDNDGMV EADDLRSLMF CDFHDPKRED
TNYREIADVD NLRMIVEIHL EEYNNISKKP MNLVLFRFAI EHISRISRIL KQPRSHALLV
GVGGSGRQSV TRLAAHMADY SVFQVEISKG YDTTEWHEDL KVILRKCAEG EMQGVFLFTD
TQIKEESFLE DVSNLLNAGE IPNLFALDEK QEICDKMRQL DRQRDKTKQT DGSPIALFNM
FIDHCRSQLH VVLAMSPIGD AFRNRLRKFP ALVNCCTIDW FQSWPEDALQ AVASRFLEEI
EMSEEIRDGC IDMCKSFHTS TIDLSKSFFV ELQRYNYVTP TSYLELISTF KLLLEKKRSE
VMKMKKRYEV GLEKLDSASS QVATMQMELE ALHPQLKVAS KEVDEMMIMI EKESVEVAKT
EKIVKADETI ANEQAMASKA IKDECDADLA GALPILESAL AALDTLTAQD ITVVKSMKSP
PAGVKLVMEA ICILKGIKAD KIPDPTGSGK KIEDFWGPAK RLLGDMRFLQ SLHEYDKDNI
PPAYMNIIRK NYIPNPDFVP EKIRNASTAA EGLCKWVIAM DSYDKVAKIV APKKIKLAAA
EGELKIAMDG LRKKQAALKE VQDKLARLQD TLELNKQKKA DLENQVDLCS KKLERAEQLI
GGLGGEKTRW SHTALELGQL YINLTGDILI SSGVVAYLGA FTSTYRQNQT KEWTTLCKGR
DIPCSDDCSL MGTLGEAVTI RTWNIAGLPS DSFSIDNGII IMNARRWPLM IDPQSQANKW
IKNMEKANSL YVIKLSEPDY VRTLENCIQF GTPVLLENVG EELDPILEPL LLKQTFKQGG
STCIRLGDST IEYAPDFRFY ITTKLRNPHY LPETSVKVTL LNFMITPEGM QDQLLGIVVA
QERPDLEEEK QALILQGAEN KRQLKEIEDK ILEVLSSSEG NILEDETAIK ILSSSKALAN
EISQKQEVAE ETEKKIDTTR MGYRPIAIHS SILFFSLADL ANIEPMYQYS LTWFINLFIL
SIENSEKSEI LAKRLQILKD HFTYSLYVNV CRSLFEKDKL LFSFCLTINL LLHERAINKA
EWRFLLTGGI GLDNPYANLC TWLPQKSWDE ICRLDDLPAF KTIRREFMRL KDGWKKVYDS
LEPHHEVFPE EWEDKANEFQ RMLIIRCLRP DKVIPMLQEF IINRLGRAFI EPPPFDLAKA
FGDSNCCAPL IFVLSPGADP MAALLKFADD QGYGGSKLSS LSLGQGQGPI AMKMLEKAVK
EGTWVVLQNC HLATSWMPTL EKVCEELSPE STHPDFRMWL TSYPSPNFPV SVLQNGVKMT
NEAPKGLRAN IIRSYLMDPI SDPEFFGSCK KPEEFKKLLY GLCFFHALVQ ERRKFGPLGW
NIPYEFNETD LRISVQQLHM FLNQYEELPY EALRYMTGEC NYGGRVTDDW DRRTLRSILN
KFFNPELVEN SDYKFDSSGI YFVPPSGDHK SYIEYTKTLP LTPAPEIFGM NANADITKDQ
SETQLLFDNI LLTQSRSAGA GAKSSDEVVN EVASDILGKL PNNFDIEAAM RRYPTTYTQS
MNTVLVQEMG RFNKLLKTIR DSCVNIQKAI KGLAVMSTDL EEVVSSILNV KIPEMWMGKS
YPSLKPLGSY VNDFLARLKF LQQWYEVGPP PVFWLSGFFF TQAFLTGAQQ NYARKYTIPI
DLLGFDYEVM EDKEYKHPPE DGVFIHGLFL DGASWNRKIK KLAESHPKIL YDTVPVMWLK
PCKRADIPKR PSYVAPLYKT SERRGVLSTT GHSTNFVIAM TLPSDQPKEH WIGRGVALLC
QLNS
