CNNM2_HUMAN
ID CNNM2_HUMAN Reviewed; 875 AA.
AC Q9H8M5; Q5T569; Q5T570; Q8WU59; Q9H952; Q9NRK5; Q9NXT4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Metal transporter CNNM2;
DE AltName: Full=Ancient conserved domain-containing protein 2;
DE AltName: Full=Cyclin-M2;
GN Name=CNNM2; Synonyms=ACDP2;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 242-875 (ISOFORM 1).
RC TISSUE=Colon, Placenta, and Teratocarcinoma;
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=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=B-cell;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 210-875 (ISOFORM 1).
RX PubMed=12657465; DOI=10.1016/s0378-1119(02)01210-6;
RA Wang C.-Y., Shi J.-D., Yang P., Kumar P.G., Li Q.-Z., Run Q.-G., Su Y.-C.,
RA Scott H.S., Kao K.-J., She J.-X.;
RT "Molecular cloning and characterization of a novel gene family of four
RT ancient conserved domain proteins (ACDP).";
RL Gene 306:37-44(2003).
RN [5]
RP TISSUE SPECIFICITY, VARIANT HOMG6 ILE-568, CHARACTERIZATION OF VARIANT
RP HOMG6 ILE-568, AND VARIANT GLN-38.
RX PubMed=21397062; DOI=10.1016/j.ajhg.2011.02.005;
RA Stuiver M., Lainez S., Will C., Terryn S., Gunzel D., Debaix H., Sommer K.,
RA Kopplin K., Thumfart J., Kampik N.B., Querfeld U., Willnow T.E., Nemec V.,
RA Wagner C.A., Hoenderop J.G., Devuyst O., Knoers N.V., Bindels R.J.,
RA Meij I.C., Muller D.;
RT "CNNM2, encoding a basolateral protein required for renal Mg2+ handling, is
RT mutated in dominant hypomagnesemia.";
RL Am. J. Hum. Genet. 88:333-343(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-761, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP INVOLVEMENT IN HOMGSMR1, VARIANTS HOMGSMR1 LYS-122; TRP-269; PHE-330 AND
RP LYS-357, AND CHARACTERIZATION OF VARIANTS HOMGSMR1 LYS-122; TRP-269 AND
RP LYS-357.
RX PubMed=24699222; DOI=10.1371/journal.pgen.1004267;
RA Arjona F.J., de Baaij J.H., Schlingmann K.P., Lameris A.L., van Wijk E.,
RA Flik G., Regele S., Korenke G.C., Neophytou B., Rust S., Reintjes N.,
RA Konrad M., Bindels R.J., Hoenderop J.G.;
RT "CNNM2 mutations cause impaired brain development and seizures in patients
RT with hypomagnesemia.";
RL PLoS Genet. 10:E1004267-E1004267(2014).
CC -!- FUNCTION: Divalent metal cation transporter. Mediates transport of
CC divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+)
CC > Ba(2+) > Cu(2+) > Fe(2+) (By similarity).
CC {ECO:0000250|UniProtKB:Q3TWN3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H8M5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H8M5-2; Sequence=VSP_027080;
CC Name=3;
CC IsoId=Q9H8M5-3; Sequence=VSP_027077, VSP_027078;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC brain, kidney and placenta, while it is weakly expressed in skeletal
CC muscle. In the kidney, it is expressed in the distal convoluted tubule
CC and the thick ascending limb of Henle loop.
CC {ECO:0000269|PubMed:21397062}.
CC -!- DISEASE: Hypomagnesemia 6 (HOMG6) [MIM:613882]: A renal disease
CC characterized by severely lowered serum magnesium levels in the absence
CC of other electrolyte disturbances. Affected individuals show an
CC inappropriately normal urinary magnesium excretion, demonstrating a
CC defect in tubular reabsorption. Age of clinical onset is highly
CC variable and some affected individuals are asymptomatic.
CC {ECO:0000269|PubMed:21397062}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Hypomagnesemia, seizures, and intellectual disability 1
CC (HOMGSMR1) [MIM:616418]: A disease characterized by renal wasting of
CC magnesium, low serum magnesium, seizures, and variable degrees of
CC delayed psychomotor development. {ECO:0000269|PubMed:24699222}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin family,
CC hence its name. However, it has no cyclin-like function in vivo.
CC -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86374.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90926.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14386.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK000071; BAA90926.1; ALT_INIT; mRNA.
DR EMBL; AK023066; BAB14386.1; ALT_INIT; mRNA.
DR EMBL; AK023479; BAB14585.1; -; mRNA.
DR EMBL; AL139817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021222; AAH21222.3; -; mRNA.
DR EMBL; AF216962; AAF86374.1; ALT_INIT; mRNA.
DR CCDS; CCDS44474.1; -. [Q9H8M5-1]
DR CCDS; CCDS44475.1; -. [Q9H8M5-2]
DR CCDS; CCDS7543.1; -. [Q9H8M5-3]
DR RefSeq; NP_060119.3; NM_017649.4. [Q9H8M5-1]
DR RefSeq; NP_951058.1; NM_199076.2. [Q9H8M5-2]
DR RefSeq; NP_951059.1; NM_199077.2. [Q9H8M5-3]
DR PDB; 4IY0; X-ray; 1.90 A; A=429-584.
DR PDB; 4IY2; X-ray; 3.60 A; A/C=430-584.
DR PDB; 4IY4; X-ray; 2.90 A; A/C=429-584.
DR PDB; 4IYS; X-ray; 1.80 A; A=430-584.
DR PDB; 6DJ3; X-ray; 2.60 A; A/B=585-722, A/B=768-822.
DR PDB; 6N7E; X-ray; 3.50 A; A/B/C/D=429-722, A/B/C/D=768-817.
DR PDBsum; 4IY0; -.
DR PDBsum; 4IY2; -.
DR PDBsum; 4IY4; -.
DR PDBsum; 4IYS; -.
DR PDBsum; 6DJ3; -.
DR PDBsum; 6N7E; -.
DR AlphaFoldDB; Q9H8M5; -.
DR SMR; Q9H8M5; -.
DR BioGRID; 120162; 48.
DR IntAct; Q9H8M5; 5.
DR STRING; 9606.ENSP00000358894; -.
DR DrugBank; DB09481; Magnesium carbonate.
DR TCDB; 1.A.112.1.6; the cyclin m mg2+ exporter (cnnm) family.
DR GlyGen; Q9H8M5; 2 sites.
DR iPTMnet; Q9H8M5; -.
DR PhosphoSitePlus; Q9H8M5; -.
DR BioMuta; CNNM2; -.
DR DMDM; 156631023; -.
DR EPD; Q9H8M5; -.
DR jPOST; Q9H8M5; -.
DR MassIVE; Q9H8M5; -.
DR MaxQB; Q9H8M5; -.
DR PaxDb; Q9H8M5; -.
DR PeptideAtlas; Q9H8M5; -.
DR PRIDE; Q9H8M5; -.
DR ProteomicsDB; 81224; -. [Q9H8M5-1]
DR ProteomicsDB; 81225; -. [Q9H8M5-2]
DR ProteomicsDB; 81226; -. [Q9H8M5-3]
DR Antibodypedia; 46052; 168 antibodies from 22 providers.
DR DNASU; 54805; -.
DR Ensembl; ENST00000369875.3; ENSP00000358891.3; ENSG00000148842.18. [Q9H8M5-3]
DR Ensembl; ENST00000369878.9; ENSP00000358894.3; ENSG00000148842.18. [Q9H8M5-1]
DR Ensembl; ENST00000433628.2; ENSP00000392875.2; ENSG00000148842.18. [Q9H8M5-2]
DR GeneID; 54805; -.
DR KEGG; hsa:54805; -.
DR MANE-Select; ENST00000369878.9; ENSP00000358894.3; NM_017649.5; NP_060119.3.
DR UCSC; uc001kwl.4; human. [Q9H8M5-1]
DR CTD; 54805; -.
DR DisGeNET; 54805; -.
DR GeneCards; CNNM2; -.
DR HGNC; HGNC:103; CNNM2.
DR HPA; ENSG00000148842; Tissue enhanced (choroid plexus, parathyroid gland).
DR MalaCards; CNNM2; -.
DR MIM; 607803; gene.
DR MIM; 613882; phenotype.
DR MIM; 616418; phenotype.
DR neXtProt; NX_Q9H8M5; -.
DR OpenTargets; ENSG00000148842; -.
DR Orphanet; 620363; Primary hypomagnesemia-generalized seizures-intellectual disability-obesity syndrome.
DR PharmGKB; PA26669; -.
DR VEuPathDB; HostDB:ENSG00000148842; -.
DR eggNOG; KOG2118; Eukaryota.
DR GeneTree; ENSGT00940000159034; -.
DR HOGENOM; CLU_011310_1_2_1; -.
DR InParanoid; Q9H8M5; -.
DR OMA; CFMITAE; -.
DR OrthoDB; 1446644at2759; -.
DR PhylomeDB; Q9H8M5; -.
DR TreeFam; TF101012; -.
DR PathwayCommons; Q9H8M5; -.
DR SignaLink; Q9H8M5; -.
DR BioGRID-ORCS; 54805; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; CNNM2; human.
DR GenomeRNAi; 54805; -.
DR Pharos; Q9H8M5; Tbio.
DR PRO; PR:Q9H8M5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H8M5; protein.
DR Bgee; ENSG00000148842; Expressed in secondary oocyte and 157 other tissues.
DR Genevisible; Q9H8M5; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IMP:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0010960; P:magnesium ion homeostasis; IMP:MGI.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR045095; ACDP.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR12064; PTHR12064; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01595; DUF21; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; CBS domain; Cell membrane;
KW Disease variant; Epilepsy; Glycoprotein; Intellectual disability;
KW Ion transport; Membrane; Phosphoprotein; Primary hypomagnesemia;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..875
FT /note="Metal transporter CNNM2"
FT /id="PRO_0000295760"
FT TOPO_DOM 1..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..875
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 251..431
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 450..511
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 518..584
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 121..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 541..552
FT /note="GKSHLAIVQRVN -> EHTNKKPKSYQH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027077"
FT VAR_SEQ 553..875
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027078"
FT VAR_SEQ 721..742
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027080"
FT VARIANT 38
FT /note="R -> Q (in dbSNP:rs76057237)"
FT /evidence="ECO:0000269|PubMed:21397062"
FT /id="VAR_065259"
FT VARIANT 122
FT /note="E -> K (in HOMGSMR1; results in reduced protein
FT membrane expression; dbSNP:rs786205909)"
FT /evidence="ECO:0000269|PubMed:24699222"
FT /id="VAR_073848"
FT VARIANT 269
FT /note="S -> W (in HOMGSMR1; results in reduced protein
FT membrane expression; decreases cellular uptake of
FT magnesium; dbSNP:rs794726858)"
FT /evidence="ECO:0000269|PubMed:24699222"
FT /id="VAR_073849"
FT VARIANT 330
FT /note="L -> F (in HOMGSMR1)"
FT /evidence="ECO:0000269|PubMed:24699222"
FT /id="VAR_073850"
FT VARIANT 357
FT /note="E -> K (in HOMGSMR1; results in decreased cellular
FT uptake of magnesium; dbSNP:rs786205910)"
FT /evidence="ECO:0000269|PubMed:24699222"
FT /id="VAR_073851"
FT VARIANT 568
FT /note="T -> I (in HOMG6; reduced activity;
FT electrophysiological analysis shows that magnesium-
FT sensitive sodium currents are significantly diminished and
FT are blocked by increased extracellular magnesium
FT concentrations; dbSNP:rs387906975)"
FT /evidence="ECO:0000269|PubMed:21397062"
FT /id="VAR_065260"
FT CONFLICT 299
FT /note="K -> N (in Ref. 1; BAB14585)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="I -> V (in Ref. 1; BAB14386)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="E -> V (in Ref. 1; BAB14386)"
FT /evidence="ECO:0000305"
FT HELIX 430..443
FT /evidence="ECO:0007829|PDB:4IYS"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:4IYS"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:4IYS"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:4IYS"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:6N7E"
FT HELIX 467..476
FT /evidence="ECO:0007829|PDB:4IYS"
FT STRAND 479..487
FT /evidence="ECO:0007829|PDB:4IYS"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:4IYS"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:4IYS"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:4IYS"
FT HELIX 511..518
FT /evidence="ECO:0007829|PDB:4IYS"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:4IYS"
FT HELIX 531..539
FT /evidence="ECO:0007829|PDB:4IYS"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:4IY0"
FT STRAND 544..552
FT /evidence="ECO:0007829|PDB:4IYS"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:4IY0"
FT STRAND 560..568
FT /evidence="ECO:0007829|PDB:4IYS"
FT HELIX 569..579
FT /evidence="ECO:0007829|PDB:4IYS"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:4IYS"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:6N7E"
FT HELIX 622..635
FT /evidence="ECO:0007829|PDB:6DJ3"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:6DJ3"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:6DJ3"
FT HELIX 646..654
FT /evidence="ECO:0007829|PDB:6DJ3"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:6DJ3"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:6DJ3"
FT TURN 667..670
FT /evidence="ECO:0007829|PDB:6DJ3"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:6DJ3"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:6DJ3"
FT STRAND 685..692
FT /evidence="ECO:0007829|PDB:6DJ3"
FT STRAND 694..698
FT /evidence="ECO:0007829|PDB:6DJ3"
FT TURN 699..702
FT /evidence="ECO:0007829|PDB:6DJ3"
FT STRAND 703..707
FT /evidence="ECO:0007829|PDB:6DJ3"
FT HELIX 716..719
FT /evidence="ECO:0007829|PDB:6DJ3"
FT TURN 775..777
FT /evidence="ECO:0007829|PDB:6DJ3"
FT STRAND 793..800
FT /evidence="ECO:0007829|PDB:6DJ3"
FT STRAND 802..808
FT /evidence="ECO:0007829|PDB:6DJ3"
FT HELIX 809..819
FT /evidence="ECO:0007829|PDB:6DJ3"
SQ SEQUENCE 875 AA; 96623 MW; 6D19F35D1B7D9A30 CRC64;
MIGCGACEPK VKMAGGQAAA ALPTWKMAAR RSLSARGRGI LQAAAGRLLP LLLLSCCCGA
GGCAAVGENE ETVIIGLRLE DTNDVSFMEG GALRVSERTR VKLRVYGQNI NNETWSRIAF
TEHERRRHSP GERGLGGPAP PEPDSGPQRC GIRTSDIIIL PHIILNRRTS GIIEIEIKPL
RKMEKSKSYY LCTSLSTPAL GAGGSGSTGG AVGGKGGSGV AGLPPPPWAE TTWIYHDGED
TKMIVGEEKK FLLPFWLQVI FISLLLCLSG MFSGLNLGLM ALDPMELRIV QNCGTEKEKN
YAKRIEPVRR QGNYLLCSLL LGNVLVNTTL TILLDDIAGS GLVAVVVSTI GIVIFGEIVP
QAICSRHGLA VGANTIFLTK FFMMMTFPAS YPVSKLLDCV LGQEIGTVYN REKLLEMLRV
TDPYNDLVKE ELNIIQGALE LRTKTVEDVM TPLRDCFMIT GEAILDFNTM SEIMESGYTR
IPVFEGERSN IVDLLFVKDL AFVDPDDCTP LKTITKFYNH PLHFVFNDTK LDAMLEEFKK
GKSHLAIVQR VNNEGEGDPF YEVLGIVTLE DVIEEIIKSE ILDETDLYTD NRTKKKVAHR
ERKQDFSAFK QTDSEMKVKI SPQLLLAMHR FLATEVEAFS PSQMSEKILL RLLKHPNVIQ
ELKYDEKNKK APEYYLYQRN KPVDYFVLIL QGKVEVEAGK EGMKFEASAF SYYGVMALTA
SPVPLSLSRT FVVSRTELLA AGSPGENKSP PRPCGLNHSD SLSRSDRIDA VTPTLGSSNN
QLNSSLLQVY IPDYSVRALS DLQFVKISRQ QYQNALMASR MDKTPQSSDS ENTKIELTLT
ELHDGLPDET ANLLNEQNCV THSKANHSLH NEGAI
