KAD8_HUMAN
ID KAD8_HUMAN Reviewed; 479 AA.
AC Q96MA6; A8K821; Q8N9W9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Adenylate kinase 8;
DE Short=AK 8;
DE EC=2.7.4.3 {ECO:0000269|PubMed:21080915};
DE EC=2.7.4.6 {ECO:0000269|PubMed:21080915, ECO:0000269|PubMed:23416111};
DE AltName: Full=ATP-AMP transphosphorylase 8;
GN Name=AK8; Synonyms=C9orf98;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CATALYTIC ACTIVITY.
RX PubMed=21080915; DOI=10.1042/bj20101443;
RA Panayiotou C., Solaroli N., Xu Y., Johansson M., Karlsson A.;
RT "The characterization of human adenylate kinases 7 and 8 demonstrates
RT differences in kinetic parameters and structural organization among the
RT family of adenylate kinase isoenzymes.";
RL Biochem. J. 433:527-534(2011).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23416111; DOI=10.1016/j.biocel.2013.02.004;
RA Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.;
RT "The human adenylate kinase 9 is a nucleoside mono- and diphosphate
RT kinase.";
RL Int. J. Biochem. Cell Biol. 45:925-931(2013).
RN [7]
RP INTERACTION WITH CFAP45 AND CFAP52, AMP-BINDING, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=33139725; DOI=10.1038/s41467-020-19113-0;
RA Dougherty G.W., Mizuno K., Noethe-Menchen T., Ikawa Y., Boldt K.,
RA Ta-Shma A., Aprea I., Minegishi K., Pang Y.P., Pennekamp P., Loges N.T.,
RA Raidt J., Hjeij R., Wallmeier J., Mussaffi H., Perles Z., Elpeleg O.,
RA Rabert F., Shiratori H., Letteboer S.J., Horn N., Young S., Struenker T.,
RA Stumme F., Werner C., Olbrich H., Takaoka K., Ide T., Twan W.K.,
RA Biebach L., Grosse-Onnebrink J., Klinkenbusch J.A., Praveen K.,
RA Bracht D.C., Hoeben I.M., Junger K., Guetzlaff J., Cindric S., Aviram M.,
RA Kaiser T., Memari Y., Dzeja P.P., Dworniczak B., Ueffing M., Roepman R.,
RA Bartscherer K., Katsanis N., Davis E.E., Amirav I., Hamada H., Omran H.;
RT "CFAP45 deficiency causes situs abnormalities and asthenospermia by
RT disrupting an axonemal adenine nucleotide homeostasis module.";
RL Nat. Commun. 11:5520-5520(2020).
CC -!- FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the
CC reversible transfer of the terminal phosphate group between nucleoside
CC triphosphates and monophosphates. Has highest activity toward AMP, and
CC weaker activity toward dAMP, CMP and dCMP. Also displays broad
CC nucleoside diphosphate kinase activity. {ECO:0000269|PubMed:21080915,
CC ECO:0000269|PubMed:23416111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000269|PubMed:21080915};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000269|PubMed:21080915, ECO:0000269|PubMed:23416111};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000269|PubMed:21080915, ECO:0000269|PubMed:23416111};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.1 uM for AMP {ECO:0000269|PubMed:21080915};
CC KM=630 uM for dAMP {ECO:0000269|PubMed:21080915};
CC KM=1.4 uM for CMP {ECO:0000269|PubMed:21080915};
CC Vmax=2400 pmol/min/ug enzyme with AMP as substrate
CC {ECO:0000269|PubMed:21080915};
CC Vmax=1360 pmol/min/ug enzyme with dAMP as substrate
CC {ECO:0000269|PubMed:21080915};
CC Vmax=190 pmol/min/ug enzyme with CMP as substrate
CC {ECO:0000269|PubMed:21080915};
CC -!- SUBUNIT: Interacts with CFAP45 and CFAP52; CFAP45 and AK8 dimerization
CC may create a cavity at the interface of the dimer that can accommodate
CC AMP. {ECO:0000269|PubMed:33139725}.
CC -!- INTERACTION:
CC Q96MA6; Q96Q83: ALKBH3; NbExp=3; IntAct=EBI-8466265, EBI-6658697;
CC Q96MA6; P55212: CASP6; NbExp=3; IntAct=EBI-8466265, EBI-718729;
CC Q96MA6; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-8466265, EBI-10171570;
CC Q96MA6; Q07002: CDK18; NbExp=3; IntAct=EBI-8466265, EBI-746238;
CC Q96MA6; P26441: CNTF; NbExp=3; IntAct=EBI-8466265, EBI-1050897;
CC Q96MA6; O14645: DNALI1; NbExp=3; IntAct=EBI-8466265, EBI-395638;
CC Q96MA6; Q9C005: DPY30; NbExp=3; IntAct=EBI-8466265, EBI-744973;
CC Q96MA6; O75460-2: ERN1; NbExp=3; IntAct=EBI-8466265, EBI-25852368;
CC Q96MA6; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-8466265, EBI-10226858;
CC Q96MA6; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-8466265, EBI-2514791;
CC Q96MA6; O00291: HIP1; NbExp=3; IntAct=EBI-8466265, EBI-473886;
CC Q96MA6; P54652: HSPA2; NbExp=3; IntAct=EBI-8466265, EBI-356991;
CC Q96MA6; O14901: KLF11; NbExp=3; IntAct=EBI-8466265, EBI-948266;
CC Q96MA6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-8466265, EBI-21591415;
CC Q96MA6; P57077-4: MAP3K7CL; NbExp=6; IntAct=EBI-8466265, EBI-10215880;
CC Q96MA6; P33993: MCM7; NbExp=4; IntAct=EBI-8466265, EBI-355924;
CC Q96MA6; Q9NPA3: MID1IP1; NbExp=3; IntAct=EBI-8466265, EBI-750096;
CC Q96MA6; P62826: RAN; NbExp=3; IntAct=EBI-8466265, EBI-286642;
CC Q96MA6; Q14498: RBM39; NbExp=3; IntAct=EBI-8466265, EBI-395290;
CC Q96MA6; Q14498-3: RBM39; NbExp=3; IntAct=EBI-8466265, EBI-6654703;
CC Q96MA6; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-8466265, EBI-2623095;
CC Q96MA6; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-8466265, EBI-2872322;
CC Q96MA6; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-8466265, EBI-745392;
CC Q96MA6; Q9H832: UBE2Z; NbExp=3; IntAct=EBI-8466265, EBI-720977;
CC Q96MA6; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-8466265, EBI-2682299;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21080915}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:33139725}.
CC Note=Located in the proximal region of respiratory cilia.
CC {ECO:0000269|PubMed:33139725}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96MA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96MA6-2; Sequence=VSP_023419;
CC -!- TISSUE SPECIFICITY: Expressed in respiratory cells (at protein level).
CC {ECO:0000269|PubMed:33139725}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AK057266; BAB71402.1; -; mRNA.
DR EMBL; AK093446; BAC04168.1; -; mRNA.
DR EMBL; AK292186; BAF84875.1; -; mRNA.
DR EMBL; AL160165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88016.1; -; Genomic_DNA.
DR EMBL; BC034776; AAH34776.1; -; mRNA.
DR EMBL; BC050576; AAH50576.1; -; mRNA.
DR CCDS; CCDS6954.1; -. [Q96MA6-1]
DR RefSeq; NP_001304887.1; NM_001317958.1. [Q96MA6-2]
DR RefSeq; NP_001304888.1; NM_001317959.1.
DR RefSeq; NP_689785.1; NM_152572.2. [Q96MA6-1]
DR AlphaFoldDB; Q96MA6; -.
DR SMR; Q96MA6; -.
DR BioGRID; 127645; 18.
DR IntAct; Q96MA6; 25.
DR MINT; Q96MA6; -.
DR STRING; 9606.ENSP00000298545; -.
DR DrugBank; DB01717; Bis(Adenosine)-5'-Pentaphosphate.
DR iPTMnet; Q96MA6; -.
DR PhosphoSitePlus; Q96MA6; -.
DR BioMuta; AK8; -.
DR DMDM; 74752032; -.
DR EPD; Q96MA6; -.
DR MassIVE; Q96MA6; -.
DR PaxDb; Q96MA6; -.
DR PeptideAtlas; Q96MA6; -.
DR PRIDE; Q96MA6; -.
DR ProteomicsDB; 77326; -. [Q96MA6-1]
DR ProteomicsDB; 77327; -. [Q96MA6-2]
DR Antibodypedia; 18213; 114 antibodies from 27 providers.
DR DNASU; 158067; -.
DR Ensembl; ENST00000298545.4; ENSP00000298545.3; ENSG00000165695.10. [Q96MA6-1]
DR GeneID; 158067; -.
DR KEGG; hsa:158067; -.
DR MANE-Select; ENST00000298545.4; ENSP00000298545.3; NM_152572.3; NP_689785.1.
DR UCSC; uc004cbu.2; human. [Q96MA6-1]
DR CTD; 158067; -.
DR DisGeNET; 158067; -.
DR GeneCards; AK8; -.
DR HGNC; HGNC:26526; AK8.
DR HPA; ENSG00000165695; Group enriched (epididymis, fallopian tube, testis).
DR MIM; 615365; gene.
DR neXtProt; NX_Q96MA6; -.
DR OpenTargets; ENSG00000165695; -.
DR PharmGKB; PA134971772; -.
DR VEuPathDB; HostDB:ENSG00000165695; -.
DR eggNOG; KOG3078; Eukaryota.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000161613; -.
DR HOGENOM; CLU_044905_0_0_1; -.
DR InParanoid; Q96MA6; -.
DR OMA; DCIRRGW; -.
DR OrthoDB; 961384at2759; -.
DR PhylomeDB; Q96MA6; -.
DR TreeFam; TF328560; -.
DR BRENDA; 2.7.4.3; 2681.
DR PathwayCommons; Q96MA6; -.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR SABIO-RK; Q96MA6; -.
DR SignaLink; Q96MA6; -.
DR BioGRID-ORCS; 158067; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; AK8; human.
DR GenomeRNAi; 158067; -.
DR Pharos; Q96MA6; Tbio.
DR PRO; PR:Q96MA6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96MA6; protein.
DR Bgee; ENSG00000165695; Expressed in right uterine tube and 134 other tissues.
DR Genevisible; Q96MA6; HS.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:GO_Central.
DR GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:UniProtKB.
DR GO; GO:0016208; F:AMP binding; IDA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004127; F:cytidylate kinase activity; IDA:UniProtKB.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IDA:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR CDD; cd01428; ADK; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR036193; ADK_active_lid_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 2.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57774; SSF57774; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..479
FT /note="Adenylate kinase 8"
FT /id="PRO_0000279383"
FT REGION 58..258
FT /note="Adenylate kinase 1"
FT /evidence="ECO:0000305|PubMed:21080915"
FT REGION 87..113
FT /note="NMP 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 177..206
FT /note="LID 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 269..471
FT /note="Adenylate kinase 2"
FT /evidence="ECO:0000305|PubMed:21080915"
FT REGION 298..327
FT /note="NMP 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 391..424
FT /note="LID 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 67..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 140..143
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 147
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 203
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 278..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 325..327
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 354..357
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 361
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT VAR_SEQ 1..204
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023419"
FT VARIANT 5
FT /note="I -> T (in dbSNP:rs2231400)"
FT /id="VAR_030873"
FT VARIANT 130
FT /note="D -> G (in dbSNP:rs17407084)"
FT /id="VAR_030874"
SQ SEQUENCE 479 AA; 54926 MW; 9E4EABA3F429B731 CRC64;
MDATIAPHRI PPEMPQYGEE NHIFELMQNM LEQLLIHQPE DPIPFMIQHL HRDNDNVPRI
VILGPPASGK TTIAMWLCKH LNSSLLTLEN LILNEFSYTA TEARRLYLQR KTVPSALLVQ
LIQERLAEED CIKQGWILDG IPETREQALR IQTLGITPRH VIVLSAPDTV LIERNLGKRI
DPQTGEIYHT TFDWPPESEI QNRLMVPEDI SELETAQKLL EYHRNIVRVI PSYPKILKVI
SADQPCVDVF YQALTYVQSN HRTNAPFTPR VLLLGPVGSG KSLQAALLAQ KYRLVNVCCG
QLLKEAVADR TTFGELIQPF FEKEMAVPDS LLMKVLSQRL DQQDCIQKGW VLHGVPRDLD
QAHLLNRLGY NPNRVFFLNV PFDSIMERLT LRRIDPVTGE RYHLMYKPPP TMEIQARLLQ
NPKDAEEQVK LKMDLFYRNS ADLEQLYGSA ITLNGDQDPY TVFEYIESGI INPLPKKIP
