ID U4U987_DENPD Unreviewed; 1001 AA.
AC U4U987;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=CNNM transmembrane domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=D910_04581 {ECO:0000313|EMBL:ERL87181.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL87181.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL87181.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ACDP family.
CC {ECO:0000256|ARBA:ARBA00010484}.
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DR EMBL; KB631924; ERL87181.1; -; Genomic_DNA.
DR AlphaFoldDB; U4U987; -.
DR STRING; 77166.U4U987; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010960; P:magnesium ion homeostasis; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR045095; ACDP.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR12064; METAL TRANSPORTER CNNM; 1.
DR PANTHER; PTHR12064:SF59; UNEXTENDED PROTEIN; 1.
DR Pfam; PF01595; CNNM; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51846; CNNM; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 347..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..522
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 769..822
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 180..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 111864 MW; 9CBAE742A48443B6 CRC64;
MFFVRSGYRL TMSANGTRSE NFRLKTMARV SSRLLNSLSC LLIFLHVAKV AGLEDDTIPA
FFKLEKKQVS NITLHDVPAF NIVLEVQGRS LYPKMRVKIT QEMAQRNAEC READFAYNIS
EIRTDSKWGQ YSLVVPQNVS GKLYFCLPHQ IVENQLGFIT PNVIDSESYK WFHQGPGIRV
PMTEEPKATN APPMVGSRAR RDENATGMLN EESIGSIRIK GLRLEASPKE IEYDENGVPG
VLADLQHTVR LFGEGFTEGM TVTFTTEKGT FGEMCYLPIA KGFPIENGSL FGNSSVQLKV
TLPVLPASAD AFYLCVKDGP ANSLKPFVHQ GDDPWMQVKT YSSLIPLWAS IVVIFVCISF
SSLFSGLNLG LMSMDKTELK ILCNTGTAKE RKYARVIQPV RNHGNYLLCS ILLGNVLVNS
IFTIILDGLT SGLIAVIFST LAIVLFGEIF PQAVCSRHGL AIGAKTIYIT KFVMFLTFPL
SYAIAKFLDC VLGEEIGNVY TRERLKELVM VTTGENDLDK DEVNIISGAL ELRKKSVAAV
MTKIEDVFML DYEAVLDFET ITEIMKSGYS RIPVFDGTRQ NIVTMLYIKD LAFVDPDDNT
PLKTLCQFYQ NPCNFVFEDV TLDVMFKIFK EGNKGHMAFV SRVNSDGEGD PFYETIGLIT
LEDVIEELIQ AEIVDETDVI TDNRTKRRRK NITSENRKDF TVFADKTDKN KVRMSPQLTL
AAYQYLSTSV EPFQVNVISE TILKRLLKQD IVCHIKKNKE WRNDPVTVIY SQGKAVDYFV
IILEGRVEVT VGKENLVFEG GPFTYFGTQS LVQTVGIESP AAPAGMGSLE SLNIDSMLRH
TFIPDYTVRA STEVMYLRIK RSLYLAAKRA TLMEKSKRDK NQTSAQLDEE IDKVLTDIAT
VDDVLEELIS NLLDATGDDD ISSGRITPRR KSSRNLQNKS QQELINQFES PKSPSHLSNA
SPPNRLSVKG GDVNGSVKGS PVDEDNMDTR GEETSLLPKK S
//
