MICA2_RAT
ID MICA2_RAT Reviewed; 1948 AA.
AC D4A1F2; F1LW55; Q498N8; Q4G091; Q80WN5;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=[F-actin]-monooxygenase MICAL2 {ECO:0000305};
DE EC=1.14.13.225 {ECO:0000250|UniProtKB:Q8BML1};
DE AltName: Full=MICAL C-terminal-like protein;
DE Short=Mical-cL;
DE AltName: Full=Molecule interacting with CasL protein 2;
DE Short=MICAL-2;
DE AltName: Full=Protein RSB-11-77;
GN Name=Mical2 {ECO:0000312|RGD:1311773}; Synonyms=Micalcl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1372-1948 (ISOFORM 6).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1376-1948 (ISOFORM 4).
RC TISSUE=Testis;
RA Liang G., Miao S.Y., Zhang X.D., Wang L.J., Wang L.F.;
RT "A new gene from rat testis cDNA library.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1677, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Methionine monooxygenase that promotes depolymerization of F-
CC actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin
CC to form methionine-sulfoxide, resulting in actin filament disassembly
CC and preventing repolymerization (By similarity). Regulates the
CC disassembly of branched actin networks also by oxidizing ARP3B-
CC containing ARP2/3 complexes leading to ARP3B dissociation from the
CC network. Acts as a key regulator of the SRF signaling pathway elicited
CC by nerve growth factor and serum: mediates oxidation and subsequent
CC depolymerization of nuclear actin, leading to increase MKL1/MRTF-A
CC presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene
CC transcription. Does not activate SRF:MKL1/MRTF-A through RhoA (By
CC similarity). {ECO:0000250|UniProtKB:O94851,
CC ECO:0000250|UniProtKB:Q8TDZ2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-
CC (R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-
CC COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044,
CC ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.13.225; Evidence={ECO:0000250|UniProtKB:O94851};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q8TDZ2};
CC -!- SUBUNIT: Interacts with PLXNA4 (By similarity). Interacts with RAB1B
CC (By similarity). Interacts with MAPK1/ERK2 (By similarity). Interacts
CC with RAB35, RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms);
CC binding to RAB35 is of low affinity compared to other Rab proteins; at
CC least in case of RAB8A may bind 2 molecules of RAB8A simultaneously
CC through a high and a low affinity binding site, respectively (By
CC similarity). May interact with MAPK1/ERK2 (By similarity).
CC {ECO:0000250|UniProtKB:O94851, ECO:0000250|UniProtKB:Q8BML1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94851}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BML1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=3;
CC IsoId=D4A1F2-3; Sequence=Displayed;
CC Name=1;
CC IsoId=D4A1F2-1; Sequence=VSP_061316, VSP_061318, VSP_061321;
CC Name=2;
CC IsoId=D4A1F2-2; Sequence=VSP_061317, VSP_061319, VSP_061320;
CC Name=4;
CC IsoId=D4A1F2-4; Sequence=VSP_061323, VSP_061324;
CC Name=5;
CC IsoId=D4A1F2-5; Sequence=VSP_061315, VSP_061322, VSP_061323,
CC VSP_061324;
CC Name=6;
CC IsoId=D4A1F2-6; Sequence=VSP_061323;
CC -!- DOMAIN: The C-terminal RAB-binding domain (RBD) (1796-1945), also
CC described as bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to predominantly RAB8A, RAB10, RAB13 and RAB15 (in their GTP-
CC bound forms). {ECO:0000250|UniProtKB:O94851}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00138.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN46735.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC098647; AAH98647.1; -; mRNA.
DR EMBL; BC100137; AAI00138.1; ALT_INIT; mRNA.
DR EMBL; AY149342; AAN46735.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001132980.1; NM_001139508.1. [D4A1F2-1]
DR RefSeq; XP_006230127.1; XM_006230065.3. [D4A1F2-2]
DR RefSeq; XP_006230128.1; XM_006230066.3. [D4A1F2-2]
DR RefSeq; XP_017444980.1; XM_017589491.1. [D4A1F2-1]
DR AlphaFoldDB; D4A1F2; -.
DR BioGRID; 265309; 1.
DR STRING; 10116.ENSRNOP00000021858; -.
DR iPTMnet; D4A1F2; -.
DR PhosphoSitePlus; D4A1F2; -.
DR PaxDb; D4A1F2; -.
DR PeptideAtlas; D4A1F2; -.
DR PRIDE; D4A1F2; -.
DR Ensembl; ENSRNOT00000021858; ENSRNOP00000021858; ENSRNOG00000016244. [D4A1F2-1]
DR Ensembl; ENSRNOT00000081595; ENSRNOP00000074877; ENSRNOG00000016244. [D4A1F2-2]
DR GeneID; 365352; -.
DR KEGG; rno:365352; -.
DR UCSC; RGD:1311773; rat.
DR CTD; 9645; -.
DR RGD; 1311773; Mical2.
DR VEuPathDB; HostDB:ENSRNOG00000016210; -.
DR eggNOG; ENOG502QWDX; Eukaryota.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000158780; -.
DR HOGENOM; CLU_000329_0_1_1; -.
DR InParanoid; D4A1F2; -.
DR OMA; HVRDNAY; -.
DR OrthoDB; 430978at2759; -.
DR PhylomeDB; D4A1F2; -.
DR TreeFam; TF336446; -.
DR PRO; PR:Q4G091; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016210; Expressed in testis and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISS:UniProtKB.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISO:RGD.
DR GO; GO:0043914; F:NADPH:sulfur oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; ISS:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR GO; GO:0010735; P:positive regulation of transcription via serum response element binding; ISS:UniProtKB.
DR GO; GO:0019417; P:sulfur oxidation; ISS:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR029939; MICAL2.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF39; PTHR23167:SF39; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; FAD; Flavoprotein;
KW LIM domain; Metal-binding; Monooxygenase; NADP; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..1948
FT /note="[F-actin]-monooxygenase MICAL2"
FT /id="PRO_0000416302"
FT DOMAIN 516..619
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 980..1042
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 2..494
FT /note="Monooxygenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT REGION 664..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1339
FT /note="Interaction with MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q8BML1"
FT REGION 1478..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1672..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 660..681
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 664..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 116..118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 123..125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 398
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 982
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 985
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1003
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1006
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1009
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1012
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1032
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1035
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94851"
FT MOD_RES 1677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..1238
FT /note="Missing (in isoform 5)"
FT /id="VSP_061315"
FT VAR_SEQ 737..964
FT /note="Missing (in isoform 1)"
FT /id="VSP_061316"
FT VAR_SEQ 928
FT /note="Missing (in isoform 2)"
FT /id="VSP_061317"
FT VAR_SEQ 1092..1189
FT /note="DEPISPKKSKSVPKPNSRPMEVEATSPRPSEWTSVRIGPGQDGQDVLAVRVL
FT VTSEDSSSDTESDSGSIIGPCTEACEERPRLPESPPLSQPLTRHIS -> GISTSFFRK
FT ALSWPLRLTRGLLNLPQSLLRWMQGLLQAAGHHVRDNAHNYCFMFELLSLGLLLLWAFS
FT EVLAAMYRESEESLESIRSWLLRFVPVKLQ (in isoform 1)"
FT /id="VSP_061318"
FT VAR_SEQ 1092..1104
FT /note="DEPISPKKSKSVP -> VRFSLPVLHPLLG (in isoform 2)"
FT /id="VSP_061319"
FT VAR_SEQ 1105..1948
FT /note="Missing (in isoform 2)"
FT /id="VSP_061320"
FT VAR_SEQ 1190..1948
FT /note="Missing (in isoform 1)"
FT /id="VSP_061321"
FT VAR_SEQ 1284
FT /note="T -> PA (in isoform 5)"
FT /id="VSP_061322"
FT VAR_SEQ 1717..1740
FT /note="QAAVRTQAGKEGSSLVSSLVLVSG -> R (in isoform 4, isoform
FT 5 and isoform 6)"
FT /id="VSP_061323"
FT VAR_SEQ 1829
FT /note="Missing (in isoform 4 and isoform 5)"
FT /id="VSP_061324"
FT CONFLICT 1377
FT /note="P -> Q (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1447
FT /note="A -> S (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1522
FT /note="A -> V (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1529..1532
FT /note="KPET -> NPEA (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1585
FT /note="A -> T (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1593..1598
FT /note="PNPILR -> SNPFFG (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1775
FT /note="R -> G (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1785
FT /note="A -> V (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1904
FT /note="E -> K (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1933
FT /note="H -> L (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1935..1948
FT /note="Missing (in Ref. 3; AAN46735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1948 AA; 217484 MW; 293DCAC4130F1ACB CRC64;
MGENEDEKQA QASQVFENFV QATTCKGTLQ AFNILTCLLD LDPLDHRNFY TQLKSKVNTW
KAKALWHKLD KRGSHKEYKR GKACSNTKCL IVGGGPCGLR TAIELAYLGA KVVVVEKRDT
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR QLQLILFKVA LMLGVEIHVN
VEFVRVREPP KDQENRKIGW RAEFLPADHA LSNFEFDVII GADGHRNTLE GFRRKEFRGK
LAIAITANFI NRNSTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDSTHYFV
MTAKKQSLLD KGVILNDYID TEMLLCAENV NQDNLLSYAR EAADFATNYQ LPSLDFAINH
NGQPDVAMFD FTSMYASENA ALMRERQAHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD
TAWMVKSWDQ GTPPLEVLAE RESLYRLLPQ TTPENINKNF EQYTLDPATR YPNLNVHCVR
PHQVKHLYIT KEMDRFPLER WGSVRRSASL SRRESDIRPN KLLTWCQQQT KGYQHVRVTD
LTTSWRSGLA LCAIIHSFRP ELINFDSLNE NDVVENNQLA FDVAKREFGI LPVTTGKEMA
STQEPDKLSM VMYLSKFYEL FRGTPLRPMD SRRKNYGENA DFGLGKTFFQ NNYLNLTLPR
KRTPRVDAQT EENDVNKRRR QGFNNLEELP AFSSRSLGSS QEYAKESGNQ NKVKYMANQL
LAKFEENTRN PSALKQDCPR VSGMGKPVLC SASRPPGTSH CPKLEESTPR LPPPLKRQFS
STVATGQVLR ELNQVPASGE CPGRPWRARA KSDLQLGGAE NLATLPPTCQ GALALSGVLR
RLQQVEEKVL QKRAQNLANR EFHTKNIKEK AAHLASMFGH GDLPQDKLLS KRVPHAHPPS
PPSCLPSPDP AAAPSPPAAD SVSPARKVLT VGKVSSGIGA AAEVLVNLYL NDHRPKTQAT
SPDLESLRKA EFPLSLGGRD TCYFCKKRVY VMERLSAEGH FFHRECFRCS VCAAILRVAA
YAFDCDEGKF YCKLHFAHCK TSSKQRKRRA ELNQQREEEG TWPEQEAARR DVPAESSCAV
AAISTPEGSP PDEPISPKKS KSVPKPNSRP MEVEATSPRP SEWTSVRIGP GQDGQDVLAV
RVLVTSEDSS SDTESDSGSI IGPCTEACEE RPRLPESPPL SQPLTRHISL RETLTQPVSL
LLHHKEPQAV PGLQRAYSLQ SPSKYQNWRR KFQSNSTPMN QRALSPPKEP PPSSSSSSPS
LPSSFSSASV PGHTTDDSSS PQVTYNLHSP QISRDDVSPT PIYLRRARAQ GITKEIPLYL
PHSPMLESTE HCLVSPDGEE LRSPEEISAS DGCQKALALG NSESTHKDSY PVSGKDPYLP
NQMLALGAAG NTGDLSEESR MGQTGGAELS KERKLGLKKL VLTEEQKTML LDWNDYTQEH
KAGERLAQEK AENGRGNSLK PICSSTLSQA VKEKLLSQKK ALGETRTPAA KAPREREVPP
PKSPLRLIAN AIFRSLLPSS EAGKKTSSKP ETKTLPRGQP HAFTRSFSFR KLGSSKDGDQ
QSPGRHMAKK ASAFFSLASP TSKAAQASDL SPPNPILRSR SLPNRPSKMF FATTSLPPSS
KVEDVPTLLE KVSLQDAAQG PKKGASHISP LGLKDKSFES FLQECKERKD IGDFFNSPKE
KGPPGNRVPS LEKLVQPVDS TSMGQVAHPS STGQDAQAAV RTQAGKEGSS LVSSLVLVSG
PGAPVTEDTS SPTSSSAEED VETQLSSRLK EKIPRRRRKL EKQMAKQEEL KRLHKAQAIQ
RQLEEVEERQ RTSEIQGVRL EKVLRGETAD SGTQDEAQLL QEWFKLVLEK NKLMRYESEL
LIMAQELELE DHQSRLEQKL RQKMLKDEGQ KDENDLKEEQ EIFEEMMQVI EQRNKLVDSL
EEQRIKERTQ DQHFENFVLS RGCQLSRT
