ID   ADA30_HUMAN             Reviewed;         790 AA.
AC   Q9UKF2; A8K8W8; Q5T3X6; Q9UKF1;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 30;
DE            Short=ADAM 30;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=ADAM30; ORFNames=UNQ2509/PRO5997;
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] (ISOFORMS ALPHA AND BETA), VARIANT PRO-359, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=10512762; DOI=10.1006/bbrc.1999.1322;
RA   Cerretti D.P., DuBose R.F., Black R.A., Nelson N.;
RT   "Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that
RT   show testis-specific gene expression.";
RL   Biochem. Biophys. Res. Commun. 263:810-815(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
RP   PRO-359.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   FUNCTION, INTERACTION WITH CTSD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND MUTAGENESIS OF HIS-338; HIS-342 AND HIS-348.
RX   PubMed=27333034; DOI=10.1016/j.ebiom.2016.06.002;
RA   Letronne F., Laumet G., Ayral A.M., Chapuis J., Demiautte F., Laga M.,
RA   Vandenberghe M.E., Malmanche N., Leroux F., Eysert F., Sottejeau Y.,
RA   Chami L., Flaig A., Bauer C., Dourlen P., Lesaffre M., Delay C., Huot L.,
RA   Dumont J., Werkmeister E., Lafont F., Mendes T., Hansmannel F., Dermaut B.,
RA   Deprez B., Herard A.S., Dhenain M., Souedet N., Pasquier F., Tulasne D.,
RA   Berr C., Hauw J.J., Lemoine Y., Amouyel P., Mann D., Deprez R., Checler F.,
RA   Hot D., Delzescaux T., Gevaert K., Lambert J.C.;
RT   "ADAM30 Downregulates APP-Linked Defects Through Cathepsin D Activation in
RT   Alzheimer's Disease.";
RL   EBioMedicine 9:278-292(2016).
CC   -!- FUNCTION: Plays a role in lysosomal amyloid precursor protein (APP)
CC       processing by cleaving and activating CTSD/cathepsin D which leads to
CC       APP degradation (PubMed:27333034). {ECO:0000269|PubMed:27333034}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with CTSD; this leads to activation of CTSD.
CC       {ECO:0000269|PubMed:27333034}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000269|PubMed:27333034}; Single-pass type I membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha;
CC         IsoId=Q9UKF2-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=Q9UKF2-2; Sequence=VSP_005494;
CC   -!- TISSUE SPECIFICITY: Expressed in brain neurons (at protein level)
CC       (PubMed:27333034). Expressed in testis (PubMed:10512762).
CC       {ECO:0000269|PubMed:10512762, ECO:0000269|PubMed:27333034}.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC       binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC       dissociation of the cysteine from the zinc ion upon the activation-
CC       peptide release activates the enzyme.
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DR   EMBL; AF171932; AAF03780.1; -; mRNA.
DR   EMBL; AF171933; AAF03781.1; -; mRNA.
DR   EMBL; AY358734; AAQ89096.1; -; mRNA.
DR   EMBL; AK292483; BAF85172.1; -; mRNA.
DR   EMBL; AL359752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS907.1; -. [Q9UKF2-1]
DR   RefSeq; NP_068566.2; NM_021794.3. [Q9UKF2-1]
DR   AlphaFoldDB; Q9UKF2; -.
DR   SMR; Q9UKF2; -.
DR   BioGRID; 116267; 72.
DR   IntAct; Q9UKF2; 14.
DR   STRING; 9606.ENSP00000358407; -.
DR   MEROPS; M12.232; -.
DR   GlyCosmos; Q9UKF2; 5 sites, No reported glycans.
DR   GlyGen; Q9UKF2; 5 sites.
DR   iPTMnet; Q9UKF2; -.
DR   PhosphoSitePlus; Q9UKF2; -.
DR   BioMuta; ADAM30; -.
DR   DMDM; 47117918; -.
DR   MassIVE; Q9UKF2; -.
DR   PaxDb; 9606-ENSP00000358407; -.
DR   PeptideAtlas; Q9UKF2; -.
DR   ProteomicsDB; 84777; -. [Q9UKF2-1]
DR   ProteomicsDB; 84778; -. [Q9UKF2-2]
DR   Antibodypedia; 20207; 92 antibodies from 22 providers.
DR   DNASU; 11085; -.
DR   Ensembl; ENST00000369400.2; ENSP00000358407.1; ENSG00000134249.7. [Q9UKF2-1]
DR   GeneID; 11085; -.
DR   KEGG; hsa:11085; -.
DR   MANE-Select; ENST00000369400.2; ENSP00000358407.1; NM_021794.4; NP_068566.2.
DR   UCSC; uc001eij.4; human. [Q9UKF2-1]
DR   AGR; HGNC:208; -.
DR   CTD; 11085; -.
DR   DisGeNET; 11085; -.
DR   GeneCards; ADAM30; -.
DR   HGNC; HGNC:208; ADAM30.
DR   HPA; ENSG00000134249; Tissue enriched (testis).
DR   MIM; 604779; gene.
DR   neXtProt; NX_Q9UKF2; -.
DR   OpenTargets; ENSG00000134249; -.
DR   PharmGKB; PA24525; -.
DR   VEuPathDB; HostDB:ENSG00000134249; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000162954; -.
DR   HOGENOM; CLU_012714_4_0_1; -.
DR   InParanoid; Q9UKF2; -.
DR   OMA; ICGRLQC; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q9UKF2; -.
DR   TreeFam; TF314733; -.
DR   PathwayCommons; Q9UKF2; -.
DR   Reactome; R-HSA-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR   SignaLink; Q9UKF2; -.
DR   BioGRID-ORCS; 11085; 12 hits in 1147 CRISPR screens.
DR   GenomeRNAi; 11085; -.
DR   Pharos; Q9UKF2; Tdark.
DR   PRO; PR:Q9UKF2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UKF2; Protein.
DR   Bgee; ENSG00000134249; Expressed in sperm and 20 other cell types or tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:1990913; C:sperm head plasma membrane; IBA:GO_Central.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR   GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR   GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF148; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 30; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   Genevisible; Q9UKF2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; EGF-like domain; Endosome;
KW   Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..198
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029136"
FT   CHAIN           199..790
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 30"
FT                   /id="PRO_0000029137"
FT   TOPO_DOM        199..687
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        688..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        709..790
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          203..393
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          399..485
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          629..663
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          732..740
FT                   /note="1"
FT   REPEAT          741..749
FT                   /note="2"
FT   REPEAT          750..758
FT                   /note="3"
FT   REPEAT          759..767
FT                   /note="4"
FT   REPEAT          768..776
FT                   /note="5"
FT   REGION          720..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..776
FT                   /note="5 X 9 AA approximate repeats"
FT   MOTIF           170..177
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        720..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        339
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        313..388
FT                   /evidence="ECO:0000250"
FT   DISULFID        353..373
FT                   /evidence="ECO:0000250"
FT   DISULFID        355..361
FT                   /evidence="ECO:0000250"
FT   DISULFID        457..477
FT                   /evidence="ECO:0000250"
FT   DISULFID        633..644
FT                   /evidence="ECO:0000250"
FT   DISULFID        638..650
FT                   /evidence="ECO:0000250"
FT   DISULFID        652..661
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         763..771
FT                   /note="Missing (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:10512762"
FT                   /id="VSP_005494"
FT   VARIANT         359
FT                   /note="L -> P (in dbSNP:rs2641348)"
FT                   /evidence="ECO:0000269|PubMed:10512762,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_024597"
FT   VARIANT         737
FT                   /note="T -> A (in dbSNP:rs35273427)"
FT                   /id="VAR_061738"
FT   MUTAGEN         338
FT                   /note="H->L: Loss of enzymatic activity; when associated
FT                   with L-342 and L-348."
FT                   /evidence="ECO:0000269|PubMed:27333034"
FT   MUTAGEN         342
FT                   /note="H->L: Loss of enzymatic activity; when associated
FT                   with L-338 and L-348."
FT                   /evidence="ECO:0000269|PubMed:27333034"
FT   MUTAGEN         348
FT                   /note="H->L: Loss of enzymatic activity; when associated
FT                   with L-338 and L-342."
FT                   /evidence="ECO:0000269|PubMed:27333034"
FT   CONFLICT        336
FT                   /note="S -> P (in Ref. 1; AAF03781)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   790 AA;  88940 MW;  42EC8A5F6B5ACDA3 CRC64;
     MRSVQIFLSQ CRLLLLLVPT MLLKSLGEDV IFHPEGEFDS YEVTIPEKLS FRGEVQGVVS
     PVSYLLQLKG KKHVLHLWPK RLLLPRHLRV FSFTEHGELL EDHPYIPKDC NYMGSVKESL
     DSKATISTCM GGLRGVFNID AKHYQIEPLK ASPSFEHVVY LLKKEQFGNQ VCGLSDDEIE
     WQMAPYENKA RLRDFPGSYK HPKYLELILL FDQSRYRFVN NNLSQVIHDA ILLTGIMDTY
     FQDVRMRIHL KALEVWTDFN KIRVGYPELA EVLGRFVIYK KSVLNARLSS DWAHLYLQRK
     YNDALAWSFG KVCSLEYAGS VSTLLDTNIL APATWSAHEL GHAVGMSHDE QYCQCRGRLN
     CIMGSGRTGF SNCSYISFFK HISSGATCLN NIPGLGYVLK RCGNKIVEDN EECDCGSTEE
     CQKDRCCQSN CKLQPGANCS IGLCCHDCRF RPSGYVCRQE GNECDLAEYC DGNSSSCPND
     VYKQDGTPCK YEGRCFRKGC RSRYMQCQSI FGPDAMEAPS ECYDAVNLIG DQFGNCEITG
     IRNFKKCESA NSICGRLQCI NVETIPDLPE HTTIISTHLQ AENLMCWGTG YHLSMKPMGI
     PDLGMINDGT SCGEGRVCFK KNCVNSSVLQ FDCLPEKCNT RGVCNNRKNC HCMYGWAPPF
     CEEVGYGGSI DSGPPGLLRG AIPSSIWVVS IIMFRLILLI LSVVFVFFRQ VIGNHLKPKQ
     EKMPLSKAKT EQEESKTKTV QEESKTKTGQ EESEAKTGQE ESKAKTGQEE SKANIESKRP
     KAKSVKKQKK
//