ID   UN13A_HUMAN             Reviewed;        1703 AA.
AC   Q9UPW8; E5RHY9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 4.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Protein unc-13 homolog A {ECO:0000305};
DE   AltName: Full=Munc13-1;
GN   Name=UNC13A {ECO:0000312|HGNC:HGNC:23150}; Synonyms=KIAA1032;
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 GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1703.
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [3]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R.;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=12871971; DOI=10.1074/jbc.m303203200;
RA   Sheu L., Pasyk E.A., Ji J., Huang X., Gao X., Varoqueaux F., Brose N.,
RA   Gaisano H.Y.;
RT   "Regulation of insulin exocytosis by Munc13-1.";
RL   J. Biol. Chem. 278:27556-27563(2003).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
RA   Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y.,
RA   Yoon T.J.;
RT   "SYT14L, especially its C2 domain, is involved in regulating melanocyte
RT   differentiation.";
RL   J. Dermatol. Sci. 72:246-251(2013).
CC   -!- FUNCTION: Plays a role in vesicle maturation during exocytosis as a
CC       target of the diacylglycerol second messenger pathway. Involved in
CC       neurotransmitter release by acting in synaptic vesicle priming prior to
CC       vesicle fusion and participates in the activity-dependent refilling of
CC       readily releasable vesicle pool (RRP). Essential for synaptic vesicle
CC       maturation in most excitatory/glutamatergic but not inhibitory/GABA-
CC       mediated synapses. Facilitates neuronal dense core vesicles fusion as
CC       well as controls the location and efficiency of their synaptic release
CC       (By similarity). Also involved in secretory granule priming in insulin
CC       secretion. Plays a role in dendrite formation by melanocytes
CC       (PubMed:23999003). {ECO:0000250|UniProtKB:Q4KUS2,
CC       ECO:0000250|UniProtKB:Q62768, ECO:0000269|PubMed:23999003}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00041};
CC   -!- SUBUNIT: Interacts with the N-termini of STX1A and/or STX1B1 and DOC2A.
CC       Interacts with BSN. Interacts with RIMS1 which recruits UNC13A to the
CC       active zone. Forms homodimers via its first C2 domain. Also interacts
CC       via this domain with the zinc finger domain of RIMS2. Part of a complex
CC       consisting of ERC2, RIMS1 and UNC13A. Also part of a complex consisting
CC       of UNC13A, RIMS2 and RAB3A (By similarity). Interacts with FBXO45 (via
CC       SRY domain); leading to the degradation of UNC13A by the proteasome (By
CC       similarity). {ECO:0000250|UniProtKB:Q4KUS2,
CC       ECO:0000250|UniProtKB:Q62768}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q62768}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q62768}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q62768}. Presynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q62768}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q62768}. Presynaptic active zone
CC       {ECO:0000250|UniProtKB:Q62768}. Note=Translocated to the plasma
CC       membrane in response to phorbol ester binding.
CC       {ECO:0000250|UniProtKB:Q62768}.
CC   -!- TISSUE SPECIFICITY: Expressed in pancreatic islet cells
CC       (PubMed:12871971). Expressed in melanocytes (PubMed:23999003).
CC       {ECO:0000269|PubMed:12871971, ECO:0000269|PubMed:23999003}.
CC   -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC       phospholipid binding. {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal region containing both MHD domains and the third
CC       C2 domain is required for synaptic vesicle priming activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
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DR   EMBL; AC008761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB028955; BAA82984.2; -; mRNA.
DR   CCDS; CCDS46013.2; -.
DR   RefSeq; NP_001073890.2; NM_001080421.2.
DR   AlphaFoldDB; Q9UPW8; -.
DR   BMRB; Q9UPW8; -.
DR   SMR; Q9UPW8; -.
DR   BioGRID; 116665; 10.
DR   IntAct; Q9UPW8; 3.
DR   STRING; 9606.ENSP00000429562; -.
DR   GlyGen; Q9UPW8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UPW8; -.
DR   PhosphoSitePlus; Q9UPW8; -.
DR   BioMuta; UNC13A; -.
DR   DMDM; 374095515; -.
DR   EPD; Q9UPW8; -.
DR   jPOST; Q9UPW8; -.
DR   MassIVE; Q9UPW8; -.
DR   MaxQB; Q9UPW8; -.
DR   PaxDb; 9606-ENSP00000429562; -.
DR   PeptideAtlas; Q9UPW8; -.
DR   ProteomicsDB; 85464; -.
DR   Antibodypedia; 43803; 41 antibodies from 19 providers.
DR   DNASU; 23025; -.
DR   Ensembl; ENST00000519716.7; ENSP00000429562.2; ENSG00000130477.16.
DR   GeneID; 23025; -.
DR   KEGG; hsa:23025; -.
DR   MANE-Select; ENST00000519716.7; ENSP00000429562.2; NM_001080421.3; NP_001073890.2.
DR   UCSC; uc060vkq.1; human.
DR   AGR; HGNC:23150; -.
DR   DisGeNET; 23025; -.
DR   GeneCards; UNC13A; -.
DR   HGNC; HGNC:23150; UNC13A.
DR   HPA; ENSG00000130477; Group enriched (brain, pituitary gland, retina).
DR   MalaCards; UNC13A; -.
DR   MIM; 609894; gene.
DR   neXtProt; NX_Q9UPW8; -.
DR   OpenTargets; ENSG00000130477; -.
DR   Orphanet; 803; Amyotrophic lateral sclerosis.
DR   PharmGKB; PA134879020; -.
DR   VEuPathDB; HostDB:ENSG00000130477; -.
DR   eggNOG; KOG1011; Eukaryota.
DR   GeneTree; ENSGT00940000161905; -.
DR   InParanoid; Q9UPW8; -.
DR   OrthoDB; 5395569at2759; -.
DR   TreeFam; TF312844; -.
DR   PathwayCommons; Q9UPW8; -.
DR   SignaLink; Q9UPW8; -.
DR   SIGNOR; Q9UPW8; -.
DR   BioGRID-ORCS; 23025; 13 hits in 1145 CRISPR screens.
DR   ChiTaRS; UNC13A; human.
DR   GenomeRNAi; 23025; -.
DR   Pharos; Q9UPW8; Tbio.
DR   PRO; PR:Q9UPW8; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9UPW8; Protein.
DR   Bgee; ENSG00000130477; Expressed in right hemisphere of cerebellum and 153 other cell types or tissues.
DR   ExpressionAtlas; Q9UPW8; baseline and differential.
DR   GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0048786; C:presynaptic active zone; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IBA:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR   GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0017075; F:syntaxin-1 binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0061789; P:dense core granule priming; IBA:GO_Central.
DR   GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR   GO; GO:0099011; P:neuronal dense core vesicle exocytosis; ISS:UniProtKB.
DR   GO; GO:0007269; P:neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB.
DR   GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IBA:GO_Central.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR   GO; GO:0016081; P:synaptic vesicle docking; IBA:GO_Central.
DR   GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR   GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR   CDD; cd20859; C1_Munc13-2-like; 1.
DR   CDD; cd08394; C2A_Munc13; 1.
DR   CDD; cd04027; C2B_Munc13; 1.
DR   CDD; cd08395; C2C_Munc13; 1.
DR   Gene3D; 1.10.357.50; -; 1.
DR   Gene3D; 1.20.58.1100; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 3.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR010439; MUN_dom.
DR   InterPro; IPR014770; Munc13_1.
DR   InterPro; IPR014772; Munc13_dom-2.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR027080; Unc-13.
DR   InterPro; IPR037302; Unc-13_C2B.
DR   PANTHER; PTHR10480; PROTEIN UNC-13 HOMOLOG; 1.
DR   PANTHER; PTHR10480:SF1; PROTEIN UNC-13 HOMOLOG A; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00168; C2; 3.
DR   Pfam; PF06292; MUN; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00239; C2; 3.
DR   SMART; SM01145; DUF1041; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 3.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   PROSITE; PS50004; C2; 3.
DR   PROSITE; PS51258; MHD1; 1.
DR   PROSITE; PS51259; MHD2; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
DR   Genevisible; Q9UPW8; HS.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW   Differentiation; Exocytosis; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT   CHAIN           1..1703
FT                   /note="Protein unc-13 homolog A"
FT                   /id="PRO_0000188573"
FT   DOMAIN          1..97
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          659..783
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          1093..1236
FT                   /note="MHD1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT   DOMAIN          1345..1512
FT                   /note="MHD2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00588"
FT   DOMAIN          1526..1653
FT                   /note="C2 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   ZN_FING         553..603
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          186..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          320..357
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        188..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..353
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         567
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         570
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         584
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         587
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         595
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         603
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         692
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         692
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         698
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         744
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         744
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         746
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         746
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         763
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62768"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62768"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62768"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62768"
FT   VARIANT         359
FT                   /note="A -> T (in dbSNP:rs34752754)"
FT                   /id="VAR_061872"
FT   CONFLICT        1034
FT                   /note="L -> P (in Ref. 2; BAA82984)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1703 AA;  193014 MW;  C8F6CEBEEF8E050B CRC64;
     MSLLCVGVKK AKFDGAQEKF NTYVTLKVQN VKSTTIAVRG SQPSWEQDFM FEINRLDLGL
     TVEVWNKGLI WDTMVGTVWI PLRTIRQSNE EGPGEWLTLD SQVIMADSEI CGTKDPTFHR
     ILLDTRFELP LDIPEEEARY WAKKLEQLNA MRDQDEYSFQ DEQDKPLPVP SNQCCNWNYF
     GWGEQHNDDP DSAVDDRDSD YRSETSNSIP PPYYTTSQPN ASVHQYSVRP PPLGSRESYS
     DSMHSYEEFS EPQALSPTGS SRYASSGELS QGSSQLSEDF DPDEHSLQGS DMEDERDRDS
     YHSCHSSVSY HKDSPRWDQD EEELEEDLED FLEEEELPED EEELEEEEEE VPDDLGSYAQ
     REDVAVAEPK DFKRISLPPA APGKEDKAPV APTEAPDMAK VAPKPATPDK VPAAEQIPEA
     EPPKDEESFR PREDEEGQEG QDSMSRAKAN WLRAFNKVRM QLQEARGEGE MSKSLWFKGG
     PGGGLIIIDS MPDIRKRKPI PLVSDLAMSL VQSRKAGITS ALASSTLNNE ELKNHVYKKT
     LQALIYPISC TTPHNFEVWT ATTPTYCYEC EGLLWGIARQ GMRCTECGVK CHEKCQDLLN
     ADCLQRAAEK SSKHGAEDRT QNIIMVLKDR MKIRERNKPE IFELIQEIFA VTKTAHTQQM
     KAVKQSVLDG TSKWSAKISI TVVCAQGLQA KDKTGSSDPY VTVQVGKTKK RTKTIYGNLN
     PVWEENFHFE CHNSSDRIKV RVWDEDDDIK SRVKQRFKRE SDDFLGQTII EVRTLSGEMD
     VWYNLDKRTD KSAVSGAIRL HISVEIKGEE KVAPYHVQYT CLHENLFHFV TDVQNNGVVK
     IPDAKGDDAW KVYYDETAQE IVDEFAMRYG VESIYQAMTH FACLSSKYMC PGVPAVMSTL
     LANINAYYAH TTASTNVSAS DRFAASNFGK ERFVKLLDQL HNSLRIDLSM YRNNFPASSP
     ERLQDLKSTV DLLTSITFFR MKVQELQSPP RASQVVKDCV KACLNSTYEY IFNNCHELYS
     REYQTDPAKK GEVLPEEQGP SIKNLDFWSK LITLIVSIIE EDKNSYTPCL NQFPQELNVG
     KISAEVMWNL FAQDMKYAME EHDKHRLCKS ADYMNLHFKV KWLYNEYVTE LPAFKDRVPE
     YPAWFEPFVI QWLDENEEVS RDFLHGALER DKKDGFQQTS EHALFSCSVV DVFSQLNQSF
     EIIKKLECPD PQIVGHYMRR FAKTISNVLL QYADIISKDF ASYCSKEKEK VPCILMNNTQ
     QLRVQLEKMF EAMGGKELDA EASDILKELQ VKLNNVLDEL SRVFATSFQP HIEECVKQMG
     DILSQVKGTG NVPASACSSV AQDADNVLQP IMDLLDSNLT LFAKICEKTV LKRVLKELWK
     LVMNTMEKTI VLPPLTDQTM IGNLLRKHGK GLEKGRVKLP SHSDGTQMIF NAAKELGQLS
     KLKDHMVREE AKSLTPKQCA VVELALDTIK QYFHAGGVGL KKTFLEKSPD LQSLRYALSL
     YTQATDLLIK TFVQTQSAQG LGVEDPVGEV SVHVELFTHP GTGEHKVTVK VVAANDLKWQ
     TSGIFRPFIE VNIIGPQLSD KKRKFATKSK NNSWAPKYNE SFQFTLSADA GPECYELQVC
     VKDYCFARED RTVGLAVLQL RELAQRGSAA CWLPLGRRIH MDDTGLTVLR ILSQRSNDEV
     AKEFVKLKSD TRSAEEGGAA PAP
//