CAPS2_MOUSE
ID CAPS2_MOUSE Reviewed; 1297 AA.
AC Q8BYR5; O08903; Q66JM7; Q6PCL7; Q76I88; Q7TMM6; Q80ZV8; Q8BL25; Q8BY04;
AC Q8K3K6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Calcium-dependent secretion activator 2;
DE AltName: Full=Calcium-dependent activator protein for secretion 2;
DE Short=CAPS-2;
GN Name=Cadps2; Synonyms=Caps2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=12659812; DOI=10.1016/s0888-7543(02)00040-x;
RA Cisternas F.A., Vincent J.B., Scherer S.W., Ray P.N.;
RT "Cloning and characterization of human CADPS and CADPS2, new members of the
RT Ca2+-dependent activator for secretion protein family.";
RL Genomics 81:279-291(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=14715936; DOI=10.1523/jneurosci.2528-03.2004;
RA Sadakata T., Mizoguchi A., Sato Y., Katoh-Semba R., Fukuda M.,
RA Mikoshiba K., Furuichi T.;
RT "The secretory granule-associated protein CAPS2 regulates neurotrophin
RT release and cell survival.";
RL J. Neurosci. 24:43-52(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 6 AND 7).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-1297 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA Radrizzani M., Cafferata E., Vila-Ortiz G., Costanzo R.V., Ortega M.J.,
RA Gonzalez-Guerrico A., Di Tella M., Pivetta O., Carminatti H.,
RA Santa-Coloma T.;
RT "Differentially expressed mRNA in mouse cerebellum during postnatal
RT development.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-1297 (ISOFORM 5), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 136-1297 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 313-1297 (ISOFORM 6).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Salivary 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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14530279; DOI=10.1074/jbc.m304727200;
RA Speidel D., Varoqueaux F., Enk C., Nojiri M., Grishanin R.N.,
RA Martin T.F.J., Hofmann K., Brose N., Reim K.;
RT "A family of Ca2+-dependent activator proteins for secretion: comparative
RT analysis of structure, expression, localization, and function.";
RL J. Biol. Chem. 278:52802-52809(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15820695; DOI=10.1016/j.neuron.2005.02.019;
RA Speidel D., Bruederle C.E., Enk C., Voets T., Varoqueaux F., Reim K.,
RA Becherer U., Fornai F., Ruggieri S., Holighaus Y., Weihe E., Bruns D.,
RA Brose N., Rettig J.;
RT "CAPS1 regulates catecholamine loading of large dense-core vesicles.";
RL Neuron 46:75-88(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-1291, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium-binding protein involved in exocytosis of vesicles
CC filled with neurotransmitters and neuropeptides. Probably acts upstream
CC of fusion in the biogenesis or maintenance of mature secretory
CC vesicles. Regulates neurotrophin release from granule cells leading to
CC regulate cell differentiation and survival during cerebellar
CC development. May specifically mediate the Ca(2+)-dependent exocytosis
CC of large dense-core vesicles (DCVs) and other dense-core vesicles.
CC -!- SUBUNIT: Homodimer. Interacts with the dopamine receptor DRD2 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8BYR5; P61750: Arf4; NbExp=2; IntAct=EBI-7569313, EBI-7569554;
CC Q8BYR5; P84084: Arf5; NbExp=5; IntAct=EBI-7569313, EBI-7569461;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Synapse {ECO:0000269|PubMed:14530279,
CC ECO:0000269|PubMed:15820695}. Note=Membrane-associated to vesicles.
CC Strongly enriched in synaptic fractions. Probably localizes to
CC different vesicles compared to CADPS. Enriched on vesicular structures
CC in the parallel fiber terminal of granule cells that are distinct from
CC synaptic vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8BYR5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BYR5-2; Sequence=VSP_016824;
CC Name=3; Synonyms=CAPS2b;
CC IsoId=Q8BYR5-3; Sequence=VSP_016819, VSP_016824;
CC Name=4;
CC IsoId=Q8BYR5-4; Sequence=VSP_016824, VSP_016826;
CC Name=5;
CC IsoId=Q8BYR5-5; Sequence=VSP_016825, VSP_016826, VSP_016827;
CC Name=6;
CC IsoId=Q8BYR5-6; Sequence=VSP_016822, VSP_016823;
CC Name=7;
CC IsoId=Q8BYR5-7; Sequence=VSP_016820, VSP_016821;
CC -!- TISSUE SPECIFICITY: Highly expressed in cerebellum. Also expressed in
CC non-neuronal tissues such as lung, spleen, testis, uterus and ovary.
CC Highly expressed in brain. In brain, it is highly expressed in
CC cerebellum, cortex, olfactory bulb, CA1/CA2 regions of the hippocampus,
CC and dentate gyrus, and weakly or not expressed in the CA3 regions of
CC the hippocampus, striatum, thalamus, superior and inferior colliculi,
CC and brain stem. Not present in adult adrenal glands. Isoform 4, but not
CC isoform 3, is highly expressed in postnatal and adult stages of
CC cerebellum. {ECO:0000269|PubMed:14530279, ECO:0000269|PubMed:15820695}.
CC -!- DEVELOPMENTAL STAGE: Expressed at stable level during brain
CC development, with a higher level in embryonic brain.
CC -!- DOMAIN: The PH domain is essential for regulated exocytosis and binds
CC phospholipids. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58720.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH59274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 6]:
CC Sequence=AAH55462.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY072800; AAL67937.1; -; mRNA.
DR EMBL; AB098623; BAD05017.1; -; mRNA.
DR EMBL; AK038568; BAC30047.1; -; mRNA.
DR EMBL; AK042634; BAC31314.1; -; mRNA.
DR EMBL; AK046596; BAC32801.1; -; mRNA.
DR EMBL; AF000969; AAB58720.2; ALT_FRAME; mRNA.
DR EMBL; BC047394; AAH47394.1; -; mRNA.
DR EMBL; BC055462; AAH55462.1; ALT_FRAME; mRNA.
DR EMBL; BC059274; AAH59274.1; ALT_INIT; mRNA.
DR EMBL; BC080854; AAH80854.1; -; mRNA.
DR CCDS; CCDS39439.1; -. [Q8BYR5-2]
DR CCDS; CCDS57411.1; -. [Q8BYR5-5]
DR CCDS; CCDS57412.1; -. [Q8BYR5-4]
DR CCDS; CCDS57413.1; -. [Q8BYR5-6]
DR RefSeq; NP_001239034.1; NM_001252105.1. [Q8BYR5-4]
DR RefSeq; XP_006505175.1; XM_006505112.1. [Q8BYR5-1]
DR AlphaFoldDB; Q8BYR5; -.
DR SMR; Q8BYR5; -.
DR BioGRID; 235999; 1.
DR IntAct; Q8BYR5; 5.
DR MINT; Q8BYR5; -.
DR STRING; 10090.ENSMUSP00000018122; -.
DR iPTMnet; Q8BYR5; -.
DR PhosphoSitePlus; Q8BYR5; -.
DR SwissPalm; Q8BYR5; -.
DR MaxQB; Q8BYR5; -.
DR PaxDb; Q8BYR5; -.
DR PeptideAtlas; Q8BYR5; -.
DR PRIDE; Q8BYR5; -.
DR ProteomicsDB; 265658; -. [Q8BYR5-1]
DR ProteomicsDB; 265659; -. [Q8BYR5-2]
DR ProteomicsDB; 265660; -. [Q8BYR5-3]
DR ProteomicsDB; 265661; -. [Q8BYR5-4]
DR ProteomicsDB; 265662; -. [Q8BYR5-5]
DR ProteomicsDB; 265663; -. [Q8BYR5-6]
DR ProteomicsDB; 265664; -. [Q8BYR5-7]
DR Antibodypedia; 31729; 63 antibodies from 24 providers.
DR DNASU; 320405; -.
DR Ensembl; ENSMUST00000018122; ENSMUSP00000018122; ENSMUSG00000017978. [Q8BYR5-2]
DR Ensembl; ENSMUST00000115356; ENSMUSP00000111013; ENSMUSG00000017978. [Q8BYR5-6]
DR Ensembl; ENSMUST00000115358; ENSMUSP00000111015; ENSMUSG00000017978. [Q8BYR5-4]
DR Ensembl; ENSMUST00000115361; ENSMUSP00000111018; ENSMUSG00000017978. [Q8BYR5-5]
DR GeneID; 320405; -.
DR KEGG; mmu:320405; -.
DR UCSC; uc009bbe.2; mouse. [Q8BYR5-4]
DR UCSC; uc009bbg.2; mouse. [Q8BYR5-5]
DR UCSC; uc009bbh.3; mouse. [Q8BYR5-6]
DR UCSC; uc009bbm.2; mouse. [Q8BYR5-7]
DR CTD; 93664; -.
DR MGI; MGI:2443963; Cadps2.
DR VEuPathDB; HostDB:ENSMUSG00000017978; -.
DR eggNOG; KOG3543; Eukaryota.
DR GeneTree; ENSGT00590000083094; -.
DR HOGENOM; CLU_007068_1_0_1; -.
DR InParanoid; Q8BYR5; -.
DR OMA; XLLCNGK; -.
DR OrthoDB; 138870at2759; -.
DR TreeFam; TF312963; -.
DR BioGRID-ORCS; 320405; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Cadps2; mouse.
DR PRO; PR:Q8BYR5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BYR5; protein.
DR Bgee; ENSMUSG00000017978; Expressed in habenula and 213 other tissues.
DR ExpressionAtlas; Q8BYR5; baseline and differential.
DR Genevisible; Q8BYR5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009267; P:cellular response to starvation; IEP:MGI.
DR GO; GO:1990504; P:dense core granule exocytosis; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR033227; CAPS.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR12166; PTHR12166; 1.
DR Pfam; PF06292; MUN; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM01145; DUF1041; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasmic vesicle; Exocytosis;
KW Lipid-binding; Membrane; Metal-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..1297
FT /note="Calcium-dependent secretion activator 2"
FT /id="PRO_0000053869"
FT DOMAIN 353..468
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 491..594
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 886..1057
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..1075
FT /note="Interaction with DRD2"
FT /evidence="ECO:0000250"
FT REGION 1275..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 26..55
FT /note="PGVSQRAPPAAAREGRRDAPGRSGGGSGGG -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12659812"
FT /id="VSP_016819"
FT VAR_SEQ 156..173
FT /note="FLKSDRVARMVQSGGCSA -> SLQSCFGTVVLSKTISLV (in isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016820"
FT VAR_SEQ 174..1297
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016821"
FT VAR_SEQ 731..768
FT /note="PDGIGTVSVEEKERFEEIKDRLSSLLENQISHFRYCFP -> FLSFFFFFFF
FT PQSCVSFRLFTEWQSVEGTQRSEHPDSN (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016822"
FT VAR_SEQ 769..1297
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016823"
FT VAR_SEQ 826
FT /note="E -> EGPAEKET (in isoform 2, isoform 3 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:12659812,
FT ECO:0000303|PubMed:14715936, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.4"
FT /id="VSP_016824"
FT VAR_SEQ 861..863
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016825"
FT VAR_SEQ 964..1004
FT /note="KNIANSLPNVALPKVPSLPLNLPQIPSFSTPPWMASLYEST -> N (in
FT isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14715936,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016826"
FT VAR_SEQ 1105
FT /note="E -> EFRNQW (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016827"
FT CONFLICT 99
FT /note="A -> V (in Ref. 3; BAC30047)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="Q -> H (in Ref. 3; BAC30047)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..134
FT /note="LN -> SQ (in Ref. 1; AAL67937)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="V -> M (in Ref. 3; BAC32801)"
FT /evidence="ECO:0000305"
FT CONFLICT 411..412
FT /note="PQ -> AK (in Ref. 4; AAB58720)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="K -> E (in Ref. 4; AAB58720)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="V -> E (in Ref. 4; AAB58720)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="R -> P (in Ref. 4; AAB58720)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="C -> F (in Ref. 4; AAB58720)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="E -> G (in Ref. 4; AAB58720)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073
FT /note="D -> N (in Ref. 4; AAB58720)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292
FT /note="D -> E (in Ref. 5; AAH59274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1297 AA; 147841 MW; 34220B10B4429D58 CRC64;
MLDPSSSEEE SDEGLEEESR EVLVAPGVSQ RAPPAAAREG RRDAPGRSGG GSGGGAARPV
SPSPSVLSEG RNEPELQLDE EQERRIRLQL YVFVVRCIAY PFNAKQPTDM ARRQQKLNKQ
QLQLLKERFQ AFLNGETQIV ADEAFCNAVR SYYEVFLKSD RVARMVQSGG CSANDFREVF
KKNIEKRVRS LPEIDGLSKE TVLSSWIAKY DAIYRGEEDL CKQPNRMTLS AVSELILSKE
QLYEMFQQIL GIKKLEHQLL YNACQLDNAD EQAAQIRREL DGRLQLAEKM AKERRFPRFI
SKEMESMYIE ELRASVNLLM ANLESLPVSK GGPEFKLQKL KRSQNSAFLD LGDENEIQLS
KSDVVLSFTL EIVIMEVQGL KSVAPNRIVY CTMEVEGGEK LQTDQAEASR PQWGTQGDFN
TTHPRPVVKV KLFTESTGVL ALEDKELGRV VLYPTSNSSK SAELHRMTVP KNSQDSDLKI
KLAVRMDKPA HMKHSGYLYA LGQKVWKRWK KRYFVLVQVS QYTFAMCSYR EKKSEPQELM
QLEGYTVDYT DPHPGLQGGQ VFFNAVKEGD TVIFASDDEQ DRILWVQAMY RATGQSYKPV
PAVQSQKLNP KGGALHADAQ LYADRFQKHG MDEFISASPC KLDHAFLFRI LQRQTLDHRL
NDSYSCLGWF SPGQVFVLDE YCARYGVRGC HRHLCYLTEL MEHSENGAVI DPTLLHYSFA
FCASHVHGNR PDGIGTVSVE EKERFEEIKD RLSSLLENQI SHFRYCFPFG RPEGALKATL
SLLERVLMKD IATPIPAEEV KKVVRKCLEK AALINYTRLT EYAKIEETMN QATPARKLEE
VLHLAELCIE VLQQNEEHHA EGREAFAWWP DLLAEHAEKF WALFTVDMDT ALEAQPQDSW
DSFPLFQLLN NFLRNDTLLC NGKFHKHLQE IFVPLVVRYV DLMESAIAQS IHRGFEQETW
QPVKNIANSL PNVALPKVPS LPLNLPQIPS FSTPPWMASL YESTNGSTTS EDLFWKLDAL
QMFVFDLHWP EQEFAHHLEQ RLKLMASDMI EACVKRTRTA FELKLQKANK TTDLRIPASV
CTMFNVLVDA KKQSTKLCAL DGGQEQQYHS KIDDLIDNTV KEIIALLVSK FVSVLEGVLS
KLSRYDEGTF FSSILSFTVK AAAKYVDVPK PGMDLADTYI MFVRQNQDIL REKVNEEMYI
EKLFDQWYSN SMKVICVWLA DRLDLQLHIY QLKTLIKIVK KTYRDFRLQG VLEGTLNSKT
YDTLHRRLTV EEATASVSEG GGLQGITMKD SDEEEEG
