UN13B_HUMAN
ID UN13B_HUMAN Reviewed; 1591 AA.
AC O14795; Q2NKJ5; Q5VYM8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein unc-13 homolog B {ECO:0000305};
DE AltName: Full=Munc13-2;
DE Short=munc13;
GN Name=UNC13B {ECO:0000312|HGNC:HGNC:12566}; Synonyms=UNC13;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=9607201; DOI=10.1046/j.1523-1755.1998.00942.x;
RA Song Y., Ailenberg M., Silverman M.;
RT "Cloning of a novel gene in the human kidney homologous to rat munc13s: its
RT potential role in diabetic nephropathy.";
RL Kidney Int. 53:1689-1695(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 SUBCELLULAR LOCATION.
RX PubMed=10233166; DOI=10.1091/mbc.10.5.1609;
RA Song Y., Ailenberg M., Silverman M.;
RT "Human munc13 is a diacylglycerol receptor that induces apoptosis and may
RT contribute to renal cell injury in hyperglycemia.";
RL Mol. Biol. Cell 10:1609-1619(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-367, AND
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND SER-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] SER-209.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays a role in vesicle maturation during exocytosis as a
CC target of the diacylglycerol second messenger pathway. Is involved in
CC neurotransmitter release by acting in synaptic vesicle priming prior to
CC vesicle fusion and participates in the activity-depending refilling of
CC readily releasable vesicle pool (RRP) (By similarity). Essential for
CC synaptic vesicle maturation in a subset of excitatory/glutamatergic but
CC not inhibitory/GABA-mediated synapses (By similarity). In collaboration
CC with UNC13A, facilitates neuronal dense core vesicles fusion as well as
CC controls the location and efficiency of their synaptic release (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z1N9}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with RIMS1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}.
CC Synapse {ECO:0000250}. Note=Localized to synapses. Translocated to the
CC plasma membrane in response to phorbol ester binding (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14795-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14795-2; Sequence=VSP_057319;
CC -!- TISSUE SPECIFICITY: Expressed in kidney cortical epithelial cells and
CC brain. {ECO:0000269|PubMed:9607201}.
CC -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC phospholipid binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
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DR EMBL; AF020202; AAC19406.1; -; mRNA.
DR EMBL; AL353795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58383.1; -; Genomic_DNA.
DR EMBL; BC111781; AAI11782.1; -; mRNA.
DR CCDS; CCDS6579.1; -. [O14795-1]
DR CCDS; CCDS83361.1; -. [O14795-2]
DR RefSeq; NP_001317582.1; NM_001330653.1. [O14795-2]
DR RefSeq; NP_006368.3; NM_006377.3. [O14795-1]
DR AlphaFoldDB; O14795; -.
DR SMR; O14795; -.
DR BioGRID; 115759; 36.
DR IntAct; O14795; 10.
DR STRING; 9606.ENSP00000367756; -.
DR iPTMnet; O14795; -.
DR PhosphoSitePlus; O14795; -.
DR BioMuta; UNC13B; -.
DR EPD; O14795; -.
DR jPOST; O14795; -.
DR MassIVE; O14795; -.
DR MaxQB; O14795; -.
DR PaxDb; O14795; -.
DR PeptideAtlas; O14795; -.
DR PRIDE; O14795; -.
DR ProteomicsDB; 48244; -. [O14795-1]
DR Antibodypedia; 11512; 186 antibodies from 29 providers.
DR DNASU; 10497; -.
DR Ensembl; ENST00000378495.7; ENSP00000367756.3; ENSG00000198722.15. [O14795-1]
DR Ensembl; ENST00000619578.4; ENSP00000479261.1; ENSG00000198722.15. [O14795-2]
DR GeneID; 10497; -.
DR KEGG; hsa:10497; -.
DR UCSC; uc003zwq.4; human. [O14795-1]
DR CTD; 10497; -.
DR DisGeNET; 10497; -.
DR GeneCards; UNC13B; -.
DR HGNC; HGNC:12566; UNC13B.
DR HPA; ENSG00000198722; Low tissue specificity.
DR MIM; 605836; gene.
DR neXtProt; NX_O14795; -.
DR OpenTargets; ENSG00000198722; -.
DR PharmGKB; PA37203; -.
DR VEuPathDB; HostDB:ENSG00000198722; -.
DR eggNOG; KOG1011; Eukaryota.
DR GeneTree; ENSGT00940000154929; -.
DR HOGENOM; CLU_001304_3_0_1; -.
DR InParanoid; O14795; -.
DR OMA; NYFGWAD; -.
DR PhylomeDB; O14795; -.
DR TreeFam; TF312844; -.
DR PathwayCommons; O14795; -.
DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR SignaLink; O14795; -.
DR SIGNOR; O14795; -.
DR BioGRID-ORCS; 10497; 7 hits in 1077 CRISPR screens.
DR ChiTaRS; UNC13B; human.
DR GeneWiki; UNC13B; -.
DR GenomeRNAi; 10497; -.
DR Pharos; O14795; Tbio.
DR PRO; PR:O14795; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O14795; protein.
DR Bgee; ENSG00000198722; Expressed in right lung and 207 other tissues.
DR ExpressionAtlas; O14795; baseline and differential.
DR Genevisible; O14795; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
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; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; ISS:ParkinsonsUK-UCL.
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; NAS:ParkinsonsUK-UCL.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; NAS:ParkinsonsUK-UCL.
DR GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; IDA:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:ParkinsonsUK-UCL.
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:0043065; P:positive regulation of apoptotic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010808; P:positive regulation of synaptic vesicle priming; ISS:ParkinsonsUK-UCL.
DR GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IBA:GO_Central.
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; ISS:ParkinsonsUK-UCL.
DR CDD; cd00029; C1; 1.
DR CDD; cd04027; C2B_Munc13; 1.
DR Gene3D; 2.60.40.150; -; 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; PTHR10480; 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; SSF49562; 3.
DR SUPFAM; SSF57889; SSF57889; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW Exocytosis; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..1591
FT /note="Protein unc-13 homolog B"
FT /id="PRO_0000188575"
FT DOMAIN 583..707
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1013..1156
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT DOMAIN 1263..1405
FT /note="MHD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00588"
FT DOMAIN 1419..1546
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 477..527
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 155..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1172..1202
FT /evidence="ECO:0000255"
FT COMPBIAS 155..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 616
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 616
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 622
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 687
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1412
FT /note="Q -> QVHDGKGIRFTANEDIRPEK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057319"
FT VARIANT 209
FT /note="P -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036615"
FT VARIANT 238
FT /note="D -> E (in dbSNP:rs35199210)"
FT /id="VAR_037273"
FT VARIANT 1232
FT /note="E -> D (in dbSNP:rs12339582)"
FT /id="VAR_037274"
FT CONFLICT 1207
FT /note="L -> P (in Ref. 1; AAC19406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1214
FT /note="V -> I (in Ref. 4; AAI11782)"
FT /evidence="ECO:0000305"
FT CONFLICT 1404
FT /note="T -> R (in Ref. 1; AAC19406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1497
FT /note="F -> L (in Ref. 1; AAC19406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1591 AA; 180679 MW; FBE8D85C55A8D780 CRC64;
MSLLCVRVKR AKFQGSPDKF NTYVTLKVQN VKSTTVAVRG DQPSWEQDFM FEISRLDLGL
SVEVWNKGLI WDTMVGTVWI ALKTIRQSDE EGPGEWSTLE AETLMKDDEI CGTRNPTPHK
ILLDTRFELP FDIPEEEARY WTYKWEQINA LGADNEYSSQ EESQRKPLPT AAAQCSFEDP
DSAVDDRDSD YRSETSNSFP PPYHTASQPN ASVHQFPVPV RSPQQLLLQG SSRDSCNDSM
QSYDLDYPER RAISPTSSSR YGSSCNVSQG SSQLSELDQY HEQDDDHRET DSIHSCHSSH
SLSRDGQAGF GEQEKPLEVT GQAEKEAACE PKEMKEDATT HPPPDLVLQK DHFLGPQESF
PEENASSPFT QARAHWIRAV TKVRLQLQEI PDDGDPSLPQ WLPEGPAGGL YGIDSMPDLR
RKKPLPLVSD LSLVQSRKAG ITSAMATRTS LKDEELKSHV YKKTLQALIY PISCTTPHNF
EVWTATTPTY CYECEGLLWG IARQGMRCSE CGVKCHEKCQ DLLNADCLQR AAEKSCKHGA
EDRTQNIIMA MKDRMKIRER NKPEIFEVIR DVFTVNKAAH VQQMKTVKQS VLDGTSKWSA
KITITVVCAQ GLQAKDKTGS SDPYVTVQVS KTKKRTKTIF GNLNPVWEEK FHFECHNSSD
RIKVRVWDED DDIKSRVKQR LKRESDDFLG QTIIEVRTLS GEMDVWYNLE KRTDKSAVSG
AIRLQISVEI KGEEKVAPYH VQYTCLHENL FHYLTDIQGS GGVRIPEARG DDAWKVYFDE
TAQEIVDEFA MRYGIESIYQ AMTHFACLSS KYMCPGVPAV MSTLLANINA YYAHTTASTN
VSASDRFAAS NFGKERFVKL LDQLHNSLRI DLSTYRNNFP AGSPERLQDL KSTVDLLTSI
TFFRMKVQEL QSPPRASQVV KDCVKACLNS TYEYIFNNCH DLYSRQYQLK QELPPEEQGP
SIRNLDFWPK LITLIVSIIE EDKNSYTPVL NQFPQELNVG KVSAEVMWHL FAQDMKYALE
EHEKDHLCKS ADYMNLHFKV KWLHNEYVRD LPVLQGQVPE YPAWFEQFVL QWLDENEDVS
LEFLRGALER DKKDGFQQTS EHALFSCSVV DVFTQLNQSF EIIRKLECPD PSILAHYMRR
FAKTIGKVLM QYADILSKDF PAYCTKEKLP CILMNNVQQL RVQLEKMFEA MGGKELDLEA
ADSLKELQVK LNTVLDELSM VFGNSFQVRI DECVRQMADI LGQVRGTGNA SPDARASAAQ
DADSVLRPLM DFLDGNLTLF ATVCEKTVLK RVLKELWRVV MNTMERMIVL PPLTDQTGTQ
LIFTAAKELS HLSKLKDHMV REETRNLTPK QCAVLDLALD TIKQYFHAGG NGLKKTFLEK
SPDLQSLRYA LSLYTQTTDT LIKTFVRSQT TQGSGVDDPV GEVSIQVDLF THPGTGEHKV
TVKVVAANDL KWQTAGMFRP FVEVTMVGPH QSDKKRKFTT KSKSNNWAPK YNETFHFLLG
NEEGPESYEL QICVKDYCFA REDRVLGLAV MPLRDVTAKG SCACWCPLGR KIHMDETGLT
ILRILSQRSN DEVAREFVKL KSESRSTEEG S
