KAD8_PIG
ID KAD8_PIG Reviewed; 479 AA.
AC A0A4X1T4U3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Adenylate kinase 8;
DE Short=AK 8;
DE EC=2.7.4.3 {ECO:0000250|UniProtKB:Q96MA6};
DE EC=2.7.4.6 {ECO:0000250|UniProtKB:Q96MA6};
DE AltName: Full=ATP-AMP transphosphorylase 8;
GN Name=AK8;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH CFAP45 AND CFAP52, AND AMP-BINDING.
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:0000250|UniProtKB:Q96MA6}.
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:0000250|UniProtKB:Q96MA6};
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:0000250|UniProtKB:Q96MA6};
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:0000250|UniProtKB:Q96MA6};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96MA6}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q96MA6}. Note=Located in the proximal region of
CC respiratory cilia. {ECO:0000250|UniProtKB:Q96MA6}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AEMK02000005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSSSCT00015082069; ENSSSCP00015033195; ENSSSCG00015061468.
DR Ensembl; ENSSSCT00015082157; ENSSSCP00015033234; ENSSSCG00015061468.
DR Ensembl; ENSSSCT00015082264; ENSSSCP00015033281; ENSSSCG00015061468.
DR Ensembl; ENSSSCT00055011492; ENSSSCP00055009090; ENSSSCG00055005898.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 1.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:GO_Central.
DR GO; GO:0005930; C:axoneme; IDA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 ATP-binding; Cell projection; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..479
FT /note="Adenylate kinase 8"
FT /id="PRO_0000454206"
FT REGION 58..258
FT /note="Adenylate kinase 1"
FT /evidence="ECO:0000250|UniProtKB:Q96MA6"
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:0000250|UniProtKB:Q96MA6"
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"
SQ SEQUENCE 479 AA; 54249 MW; 28B498BD9728C26E CRC64;
MDATTAPHRI PPEMPQYGEA NHIFEMMQNM LEQLLIHQPT DPIPFMIDHL QLDNDYVPKI
LVLGPPASGK TTVAMWLCKH LRSNLLSVEN LIARQFSSLA AGARQHYQKF KTLPSGLLVR
LVQARLREED CVTRGWILDG IPETREQALL LQTLGIAPRH VIVLSAPDTV LIERNLGKRV
DPLTGEVYHT TFDWPPQPEI QNRLLVPAGI SEGETARKLL EFHRNIVRIA PSYPKILRVI
PADQPCVDVF CQALTYVQTI HRSNAPFTPR VLLLGPMGSG KSLQAALLAQ KYGLVNVCCG
QLLKEAVADK SKYGKVILSF FEKEIAVPDS IIMKVLGRRL DQQDCVERGW VLHGFPRDLD
QAHMLNSLGY KPNRVFFLNV PFDSILERLT LRRTDPVTGE RYHLMYKPPP TVEIQARLLQ
NPKDTEEQVK LKMDLFCRTS AELEQFYQPV LPLNGDQDPY TVFEHLESGI INPLPNKVP
