DOC2A_HUMAN
ID DOC2A_HUMAN Reviewed; 400 AA.
AC Q14183; B4DEJ2; H3BNH6; Q6P4G4; Q7Z5G0; Q8IVX0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 5.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Double C2-like domain-containing protein alpha;
DE Short=Doc2;
DE Short=Doc2-alpha;
GN Name=DOC2A;
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] (ISOFORM 1), VARIANT SER-48, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7826360; DOI=10.1006/bbrc.1995.1062;
RA Orita S., Sasaki T., Naito A., Maeda M., Igarashi H., Takai Y.;
RT "Doc2, a novel synaptic vesicle protein with two repeated C2-like
RT domains.";
RL Biochem. Biophys. Res. Commun. 206:439-448(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-48.
RC TISSUE=Brain, and Mammary gland;
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 TISSUE SPECIFICITY.
RX PubMed=8554557; DOI=10.1006/bbrc.1995.2876;
RA Sakaguchi G., Orita S., Maeda M., Igarashi H., Takai Y.;
RT "Molecular cloning of an isoform of Doc2 having two C2-like domains.";
RL Biochem. Biophys. Res. Commun. 217:1053-1061(1995).
RN [6]
RP FUNCTION, AND INTERACTION WITH UNC13A.
RX PubMed=9736751; DOI=10.1073/pnas.95.19.11418;
RA Mochida S., Orita S., Sakaguchi G., Sasaki T., Takai Y.;
RT "Role of the Doc2 alpha-Munc13-1 interaction in the neurotransmitter
RT release process.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11418-11422(1998).
RN [7]
RP FUNCTION, AND INTERACTION WITH DYNLT1.
RX PubMed=9804756; DOI=10.1074/jbc.273.46.30065;
RA Nagano F., Orita S., Sasaki T., Naito A., Sakaguchi G., Maeda M.,
RA Watanabe T., Kominami E., Uchiyama Y., Takai Y.;
RT "Interaction of Doc2 with tctex-1, a light chain of cytoplasmic dynein.
RT Implication in dynein-dependent vesicle transport.";
RL J. Biol. Chem. 273:30065-30068(1998).
RN [8]
RP FUNCTION, AND INTERACTION WITH UNC13D.
RX PubMed=18354201; DOI=10.4049/jimmunol.180.7.4774;
RA Higashio H., Nishimura N., Ishizaki H., Miyoshi J., Orita S., Sakane A.,
RA Sasaki T.;
RT "Doc2 alpha and Munc13-4 regulate Ca(2+) -dependent secretory lysosome
RT exocytosis in mast cells.";
RL J. Immunol. 180:4774-4784(2008).
CC -!- FUNCTION: Calcium sensor which most probably regulates fusion of
CC vesicles with membranes. Binds calcium and phospholipids. May be
CC involved in calcium dependent neurotransmitter release through the
CC interaction with UNC13A. May be involved in calcium-dependent
CC spontaneous release of neurotransmitter in absence of action potentials
CC in neuronal cells. Regulates Ca(2+)-dependent secretory lysosome
CC exocytosis in mast cells. {ECO:0000269|PubMed:18354201,
CC ECO:0000269|PubMed:9736751, ECO:0000269|PubMed:9804756}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts (via N-terminus) with UNC13A. Interacts with
CC cytoplasmic dynein light chain DYNLT1. Interacts with UNC13D.
CC {ECO:0000269|PubMed:18354201, ECO:0000269|PubMed:9736751,
CC ECO:0000269|PubMed:9804756}.
CC -!- INTERACTION:
CC Q14183; Q8TF42: UBASH3B; NbExp=5; IntAct=EBI-20861623, EBI-1380492;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. Cytoplasmic vesicle,
CC secretory vesicle, synaptic vesicle membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}. Synapse, synaptosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14183-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14183-2; Sequence=VSP_056977, VSP_056978, VSP_056979;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Also expressed in
CC testis. {ECO:0000269|PubMed:7826360, ECO:0000269|PubMed:8554557}.
CC -!- DOMAIN: C2 domain 1 is involved in binding calcium and phospholipids.
CC {ECO:0000250}.
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DR EMBL; D31897; BAA06695.1; -; mRNA.
DR EMBL; AK293651; BAG57103.1; -; mRNA.
DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041769; AAH41769.2; -; mRNA.
DR EMBL; BC055284; AAH55284.1; -; mRNA.
DR EMBL; BC063436; AAH63436.1; -; mRNA.
DR CCDS; CCDS10666.1; -. [Q14183-1]
DR PIR; JC2473; JC2473.
DR RefSeq; NP_001268991.1; NM_001282062.1. [Q14183-1]
DR RefSeq; NP_001268992.1; NM_001282063.1. [Q14183-1]
DR RefSeq; NP_001268997.1; NM_001282068.1. [Q14183-1]
DR RefSeq; NP_003577.2; NM_003586.2. [Q14183-1]
DR RefSeq; XP_011544277.1; XM_011545975.1. [Q14183-1]
DR RefSeq; XP_016879265.1; XM_017023776.1.
DR RefSeq; XP_016879266.1; XM_017023777.1.
DR PDB; 4MJJ; X-ray; 2.00 A; A=81-217.
DR PDBsum; 4MJJ; -.
DR AlphaFoldDB; Q14183; -.
DR SMR; Q14183; -.
DR BioGRID; 114026; 14.
DR IntAct; Q14183; 9.
DR STRING; 9606.ENSP00000340017; -.
DR iPTMnet; Q14183; -.
DR PhosphoSitePlus; Q14183; -.
DR SwissPalm; Q14183; -.
DR BioMuta; DOC2A; -.
DR DMDM; 150421541; -.
DR jPOST; Q14183; -.
DR MassIVE; Q14183; -.
DR MaxQB; Q14183; -.
DR PaxDb; Q14183; -.
DR PeptideAtlas; Q14183; -.
DR PRIDE; Q14183; -.
DR ProteomicsDB; 3964; -.
DR ProteomicsDB; 59901; -. [Q14183-1]
DR Antibodypedia; 26947; 134 antibodies from 24 providers.
DR DNASU; 8448; -.
DR Ensembl; ENST00000350119.9; ENSP00000340017.4; ENSG00000149927.18. [Q14183-1]
DR Ensembl; ENST00000564944.5; ENSP00000455196.1; ENSG00000149927.18. [Q14183-1]
DR Ensembl; ENST00000564979.5; ENSP00000455624.1; ENSG00000149927.18. [Q14183-1]
DR Ensembl; ENST00000566310.5; ENSP00000454857.1; ENSG00000149927.18. [Q14183-2]
DR Ensembl; ENST00000616445.4; ENSP00000482870.1; ENSG00000149927.18. [Q14183-1]
DR GeneID; 8448; -.
DR KEGG; hsa:8448; -.
DR MANE-Select; ENST00000350119.9; ENSP00000340017.4; NM_003586.3; NP_003577.2.
DR UCSC; uc002dvn.4; human. [Q14183-1]
DR CTD; 8448; -.
DR DisGeNET; 8448; -.
DR GeneCards; DOC2A; -.
DR HGNC; HGNC:2985; DOC2A.
DR HPA; ENSG00000149927; Tissue enhanced (brain, testis).
DR MIM; 604567; gene.
DR neXtProt; NX_Q14183; -.
DR OpenTargets; ENSG00000149927; -.
DR PharmGKB; PA27451; -.
DR VEuPathDB; HostDB:ENSG00000149927; -.
DR eggNOG; KOG1013; Eukaryota.
DR GeneTree; ENSGT00940000159141; -.
DR HOGENOM; CLU_023008_3_0_1; -.
DR InParanoid; Q14183; -.
DR OMA; SPMTVRK; -.
DR OrthoDB; 374694at2759; -.
DR PhylomeDB; Q14183; -.
DR TreeFam; TF351844; -.
DR PathwayCommons; Q14183; -.
DR SignaLink; Q14183; -.
DR BioGRID-ORCS; 8448; 15 hits in 1070 CRISPR screens.
DR ChiTaRS; DOC2A; human.
DR GeneWiki; DOC2A; -.
DR GenomeRNAi; 8448; -.
DR Pharos; Q14183; Tbio.
DR PRO; PR:Q14183; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q14183; protein.
DR Bgee; ENSG00000149927; Expressed in right frontal lobe and 105 other tissues.
DR ExpressionAtlas; Q14183; baseline and differential.
DR Genevisible; Q14183; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IMP:UniProtKB.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:Ensembl.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR014638; Doc2.
DR InterPro; IPR030535; Doc2a/b.
DR InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR InterPro; IPR001565; Synaptotagmin.
DR PANTHER; PTHR45729; PTHR45729; 1.
DR PANTHER; PTHR45729:SF1; PTHR45729:SF1; 1.
DR Pfam; PF00168; C2; 2.
DR PIRSF; PIRSF036931; Doc2; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium/phospholipid-binding;
KW Cytoplasmic vesicle; Exocytosis; Lysosome; Membrane; Metal-binding;
KW Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..400
FT /note="Double C2-like domain-containing protein alpha"
FT /id="PRO_0000079965"
FT DOMAIN 89..211
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 251..384
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..89
FT /note="Interaction with UNC13D and DYNLT1"
FT /evidence="ECO:0000269|PubMed:18354201,
FT ECO:0000269|PubMed:9804756"
FT REGION 215..400
FT /note="Interaction with UNC13D"
FT /evidence="ECO:0000269|PubMed:18354201"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056977"
FT VAR_SEQ 271..281
FT /note="GILRCAHLAAM -> PEARCGQEIQA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056978"
FT VAR_SEQ 282..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056979"
FT VARIANT 48
FT /note="G -> S (in dbSNP:rs1140239)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7826360"
FT /id="VAR_019656"
FT CONFLICT 92
FT /note="T -> K (in Ref. 1; BAA06695)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..109
FT /note="CS -> VC (in Ref. 1; BAA06695)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="E -> D (in Ref. 1; BAA06695)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="P -> R (in Ref. 1; BAA06695)"
FT /evidence="ECO:0000305"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:4MJJ"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:4MJJ"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:4MJJ"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:4MJJ"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4MJJ"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4MJJ"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:4MJJ"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:4MJJ"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:4MJJ"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:4MJJ"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4MJJ"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4MJJ"
SQ SEQUENCE 400 AA; 43959 MW; 2E61A459AC373C6C CRC64;
MRGRRGDRMT INIQEHMAIN VCPGPIRPIR QISDYFPRGP GPEGGGGGGG EAPAHLVPLA
LAPPAALLGA TTPEDGAEVD SYDSDDATAL GTLEFDLLYD RASCTLHCSI LRAKGLKPMD
FNGLADPYVK LHLLPGACKA NKLKTKTQRN TLNPVWNEDL TYSGITDDDI THKVLRIAVC
DEDKLSHNEF IGEIRVPLRR LKPSQKKHFN ICLERQVPLA SPSSMSAALR GISCYLKELE
QAEQGQGLLE ERGRILLSLS YSSRRRGLLV GILRCAHLAA MDVNGYSDPY VKTYLRPDVD
KKSKHKTCVK KKTLNPEFNE EFFYEIELST LATKTLEVTV WDYDIGKSND FIGGVSLGPG
ARGEARKHWS DCLQQPDAAL ERWHTLTSEL PPAAGALSSA
