REV1_ARATH
ID REV1_ARATH Reviewed; 1105 AA.
AC A3EWL3; A3EWL4; A3EWL5; A3EWL6; A3EWL7; A3EWL8; O48585; Q5FBB9; Q8RXL1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=DNA repair protein REV1;
DE Short=AtREV1;
DE EC=2.7.7.-;
DE AltName: Full=Rev1-like terminal deoxycytidyl transferase;
GN Name=REV1; OrderedLocusNames=At5g44750; ORFNames=K23L20.9, T19K24.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DISRUPTION PHENOTYPE.
RX PubMed=15908599; DOI=10.1104/pp.105.060236;
RA Takahashi S., Sakamoto A., Sato S., Kato T., Tabata S., Tanaka A.;
RT "Roles of Arabidopsis AtREV1 and AtREV7 in translesion synthesis.";
RL Plant Physiol. 138:870-881(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6 AND 7).
RC STRAIN=cv. Columbia;
RX DOI=10.1016/j.plantsci.2009.01.018;
RA Santiago M.J., Alejandre-Duran E., Ruiz-Rubio M.;
RT "Alternative splicing of two translesion synthesis DNA polymerases from
RT Arabidopsis thaliana.";
RL Plant Sci. 176:591-596(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 924-1105 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP FUNCTION, AND COFACTOR.
RX PubMed=17827267; DOI=10.1104/pp.107.101980;
RA Takahashi S., Sakamoto A.N., Tanaka A., Shimizu K.;
RT "AtREV1, a Y-family DNA polymerase in Arabidopsis, has deoxynucleotidyl
RT transferase activity in vitro.";
RL Plant Physiol. 145:1052-1060(2007).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18339443; DOI=10.1016/j.jplph.2007.11.012;
RA Jesus Santiago M., Alejandre-Duran E., Munoz-Serrano A., Ruiz-Rubio M.;
RT "Two translesion synthesis DNA polymerase genes, AtPOLH and AtREV1, are
RT involved in development and UV light resistance in Arabidopsis.";
RL J. Plant Physiol. 165:1582-1591(2008).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21030509; DOI=10.1104/pp.110.166082;
RA Nakagawa M., Takahashi S., Tanaka A., Narumi I., Sakamoto A.N.;
RT "Role of AtPolzeta, AtRev1, and AtPoleta in UV light-induced mutagenesis in
RT Arabidopsis.";
RL Plant Physiol. 155:414-420(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21455019; DOI=10.4161/psb.6.5.15124;
RA Nakagawa M., Takahashi S., Narumi I., Sakamoto A.N.;
RT "Role of AtPolzeta, AtRev1 and AtPoleta in gamma ray-induced mutagenesis.";
RL Plant Signal. Behav. 6:728-731(2011).
CC -!- FUNCTION: Deoxycytidyl transferase involved in DNA repair and
CC translesion synthesis (TLS). Transfers a dCMP residue from dCTP to the
CC 3'-end of a DNA primer in a template-dependent reaction. Mediates also
CC the insertion of dTMP or dGMP when the opposite base is G, and, with a
CC low efficiency, dGMP insertions opposite G, T, and C, dAMP insertions
CC opposite G, A, and T, and dTMP insertion opposite A. May assist in the
CC first step in the bypass of abasic lesions by the insertion of a
CC nucleotide opposite the lesion. Required for normal induction of
CC mutations by physical and chemical agents (e.g. UV and gamma ray),
CC mostly via G to T transversions, and of spontaneous mutations in
CC somatic cells. Confers resistance to ultraviolet-B (UV-B) and various
CC DNA cross-linkers (e.g. mitomycin C MMC and cisplatin). Promotes stem
CC growth. {ECO:0000269|PubMed:17827267, ECO:0000269|PubMed:18339443,
CC ECO:0000269|PubMed:21030509, ECO:0000269|PubMed:21455019}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17827267};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17827267};
CC Note=Mn(2+) ions. Can also use Mg(2+) ions with a lower efficiency.
CC {ECO:0000269|PubMed:17827267};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=AtREV1-1105;
CC IsoId=A3EWL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A3EWL3-2; Sequence=VSP_042707;
CC Name=3; Synonyms=AtREV1-431;
CC IsoId=A3EWL3-3; Sequence=VSP_042704;
CC Name=4; Synonyms=AtREV1-630;
CC IsoId=A3EWL3-4; Sequence=VSP_042706;
CC Name=5; Synonyms=AtREV1-651;
CC IsoId=A3EWL3-5; Sequence=VSP_042708;
CC Name=6; Synonyms=AtREV1-436;
CC IsoId=A3EWL3-6; Sequence=VSP_042705;
CC Name=7; Synonyms=AtREV1-444;
CC IsoId=A3EWL3-7; Sequence=VSP_042703, VSP_042708;
CC -!- DOMAIN: The C-terminal domain is necessary for protein interactions.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced UV light- and gamma ray-induced mutation
CC frequency. Slightly sensitive to ultraviolet-B (UV-B) and DNA cross-
CC linkers (e.g. mitomycin C MMC and cisplatin). Lower germination rate.
CC {ECO:0000269|PubMed:15908599, ECO:0000269|PubMed:18339443,
CC ECO:0000269|PubMed:21030509, ECO:0000269|PubMed:21455019}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79145.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB08828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB187523; BAD89586.1; -; mRNA.
DR EMBL; EF016093; ABN48548.1; -; mRNA.
DR EMBL; EF016094; ABN48549.1; -; mRNA.
DR EMBL; EF016095; ABN48550.1; -; mRNA.
DR EMBL; EF016096; ABN48551.1; -; mRNA.
DR EMBL; EF016097; ABN48552.1; -; mRNA.
DR EMBL; EF016098; ABN48553.1; -; mRNA.
DR EMBL; AB016874; BAB08828.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC002342; AAC79145.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95156.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95157.1; -; Genomic_DNA.
DR EMBL; AY080825; AAL87302.1; -; mRNA.
DR RefSeq; NP_001119373.1; NM_001125901.2. [A3EWL3-1]
DR RefSeq; NP_199288.4; NM_123842.5. [A3EWL3-2]
DR AlphaFoldDB; A3EWL3; -.
DR SMR; A3EWL3; -.
DR STRING; 3702.AT5G44750.2; -.
DR PaxDb; A3EWL3; -.
DR PRIDE; A3EWL3; -.
DR ProteomicsDB; 236891; -. [A3EWL3-1]
DR EnsemblPlants; AT5G44750.1; AT5G44750.1; AT5G44750. [A3EWL3-2]
DR EnsemblPlants; AT5G44750.2; AT5G44750.2; AT5G44750. [A3EWL3-1]
DR GeneID; 834504; -.
DR Gramene; AT5G44750.1; AT5G44750.1; AT5G44750. [A3EWL3-2]
DR Gramene; AT5G44750.2; AT5G44750.2; AT5G44750. [A3EWL3-1]
DR KEGG; ath:AT5G44750; -.
DR Araport; AT5G44750; -.
DR TAIR; locus:2156319; AT5G44750.
DR eggNOG; KOG2093; Eukaryota.
DR InParanoid; A3EWL3; -.
DR OMA; CDEMFVE; -.
DR OrthoDB; 299766at2759; -.
DR PhylomeDB; A3EWL3; -.
DR PRO; PR:A3EWL3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; A3EWL3; baseline and differential.
DR Genevisible; A3EWL3; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0017125; F:deoxycytidyl transferase activity; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0070987; P:error-free translesion synthesis; IBA:GO_Central.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR012112; REV1.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR PIRSF; PIRSF036573; REV1; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA damage; DNA repair; DNA synthesis; DNA-binding;
KW Magnesium; Manganese; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..1105
FT /note="DNA repair protein REV1"
FT /id="PRO_0000416595"
FT DOMAIN 83..174
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 375..556
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..340
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 556..559
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 612..620
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 775..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1103
FT /note="Protein interaction domain; mediates interaction
FT with DNA polymerase zeta"
FT /evidence="ECO:0000250"
FT MOTIF 953..961
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 198..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 335
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 379..383
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 416..422
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT SITE 384
FT /note="Substrate discrimination"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT SITE 676
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 333..539
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_042703"
FT VAR_SEQ 426..1105
FT /note="VKAGMFVRHAKDLCPQLVIVPYNFEAYEEVADQFYDILHRHCRKVQALSCDE
FT AFLDVSDLSDVETEVLASTIRNEILETTGCSASAGIGGTMLMARLATRVAKPAGQLYIS
FT AEKVEEFLDQLPVGTLPGVGSVLKEKLVKQNIQTCGQLRLISKDSLQKDFGVKTGEMLW
FT SYSRGLDLRSVTAVQESKSIGAEVNWGVRFRDQQDVFILVQHFLQCLCKEVSLRLQGCE
FT MIGRTFTLKIKKRKKDAEEPTKYMGCGDCDNLSRSITVPAATDDIEVLQRISKKLFGSF
FT CLDVKEVRGVGLQVSKLDSADPSNKGSRTLKSWLSSAPAVVQIEQDDNVFAAKVRENSD
FT CNRPVTGGVSRLRESNSEESSIQSGDTNSSLPPMCYLDMEVLENLPPELLSELDGTYGG
FT KLFELIEKKRGKRRINCNSPHVSLDGTAASIKELKSLSVKIHGLSTSGEKEYKEPYVPH
FT PSIARTSNQHTIEMTDLLPSSLSQVDVSVLQELPEELRADVLGAFPSHRRQQSSSDVPK
FT ETCKKQDEEPIDLKGTENEIGLSFSSLWFGNPPLWTEKFKVSGNCTMEKLSAIYFKVAQ
FT SRPMLSLVLQHAISEMSSFPDAASASDLDKAIYDVCELLKQYINLKVGGDIEEIYLCFR
FT LLKRLAARSQLFLQVYEILSPFIQASISEHYGGSLSIP -> LSYTKE (in
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_042704"
FT VAR_SEQ 430..1105
FT /note="MFVRHAKDLCPQLVIVPYNFEAYEEVADQFYDILHRHCRKVQALSCDEAFLD
FT VSDLSDVETEVLASTIRNEILETTGCSASAGIGGTMLMARLATRVAKPAGQLYISAEKV
FT EEFLDQLPVGTLPGVGSVLKEKLVKQNIQTCGQLRLISKDSLQKDFGVKTGEMLWSYSR
FT GLDLRSVTAVQESKSIGAEVNWGVRFRDQQDVFILVQHFLQCLCKEVSLRLQGCEMIGR
FT TFTLKIKKRKKDAEEPTKYMGCGDCDNLSRSITVPAATDDIEVLQRISKKLFGSFCLDV
FT KEVRGVGLQVSKLDSADPSNKGSRTLKSWLSSAPAVVQIEQDDNVFAAKVRENSDCNRP
FT VTGGVSRLRESNSEESSIQSGDTNSSLPPMCYLDMEVLENLPPELLSELDGTYGGKLFE
FT LIEKKRGKRRINCNSPHVSLDGTAASIKELKSLSVKIHGLSTSGEKEYKEPYVPHPSIA
FT RTSNQHTIEMTDLLPSSLSQVDVSVLQELPEELRADVLGAFPSHRRQQSSSDVPKETCK
FT KQDEEPIDLKGTENEIGLSFSSLWFGNPPLWTEKFKVSGNCTMEKLSAIYFKVAQSRPM
FT LSLVLQHAISEMSSFPDAASASDLDKAIYDVCELLKQYINLKVGGDIEEIYLCFRLLKR
FT LAARSQLFLQVYEILSPFIQASISEHYGGSLSIP -> IAEKSRR (in isoform
FT 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_042705"
FT VAR_SEQ 613..1105
FT /note="KSIGAEVNWGVRFRDQQDVFILVQHFLQCLCKEVSLRLQGCEMIGRTFTLKI
FT KKRKKDAEEPTKYMGCGDCDNLSRSITVPAATDDIEVLQRISKKLFGSFCLDVKEVRGV
FT GLQVSKLDSADPSNKGSRTLKSWLSSAPAVVQIEQDDNVFAAKVRENSDCNRPVTGGVS
FT RLRESNSEESSIQSGDTNSSLPPMCYLDMEVLENLPPELLSELDGTYGGKLFELIEKKR
FT GKRRINCNSPHVSLDGTAASIKELKSLSVKIHGLSTSGEKEYKEPYVPHPSIARTSNQH
FT TIEMTDLLPSSLSQVDVSVLQELPEELRADVLGAFPSHRRQQSSSDVPKETCKKQDEEP
FT IDLKGTENEIGLSFSSLWFGNPPLWTEKFKVSGNCTMEKLSAIYFKVAQSRPMLSLVLQ
FT HAISEMSSFPDAASASDLDKAIYDVCELLKQYINLKVGGDIEEIYLCFRLLKRLAARSQ
FT LFLQVYEILSPFIQASISEHYGGSLSIP -> STLPPMPMQRSFFASARM (in
FT isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_042706"
FT VAR_SEQ 631..634
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15908599"
FT /id="VSP_042707"
FT VAR_SEQ 636..1105
FT /note="QHFLQCLCKEVSLRLQGCEMIGRTFTLKIKKRKKDAEEPTKYMGCGDCDNLS
FT RSITVPAATDDIEVLQRISKKLFGSFCLDVKEVRGVGLQVSKLDSADPSNKGSRTLKSW
FT LSSAPAVVQIEQDDNVFAAKVRENSDCNRPVTGGVSRLRESNSEESSIQSGDTNSSLPP
FT MCYLDMEVLENLPPELLSELDGTYGGKLFELIEKKRGKRRINCNSPHVSLDGTAASIKE
FT LKSLSVKIHGLSTSGEKEYKEPYVPHPSIARTSNQHTIEMTDLLPSSLSQVDVSVLQEL
FT PEELRADVLGAFPSHRRQQSSSDVPKETCKKQDEEPIDLKGTENEIGLSFSSLWFGNPP
FT LWTEKFKVSGNCTMEKLSAIYFKVAQSRPMLSLVLQHAISEMSSFPDAASASDLDKAIY
FT DVCELLKQYINLKVGGDIEEIYLCFRLLKRLAARSQLFLQVYEILSPFIQASISEHYGG
FT SLSIP -> NNVLLFFPKHYSFDVS (in isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_042708"
SQ SEQUENCE 1105 AA; 122233 MW; 77C0814E4CAD79DE CRC64;
MKRSLGSNSS NNSGSGSNKK SKKNNNPSNQ KTLGAAWGAA SSRSSFRSSP FSDFGSYMEV
KNRKLQNQFE TEASAASRGV SGSEKLIFQG VSIFVDGFTI PSHQELKGYM MKYGGRFENY
FSRRSVTHII CSNLPDSKVK NLRTFSRGLP VVKPTWIVDS ISANRLLGWV PYQLDQLNDT
QPKLSAFFAP RSHLTPQMAS PVTSFQPDTG YSEAEEGSSI RADDSEEARD HIDDEIDGVY
IENTTPELTE QTGTGDLKSS EMNAEGLGNY DIEEKEVSSE LQSTTNLHST SDNKSVHANG
KNGGKSIATA AGSSTRRHST LEDPNFVENY FKNSRLHFIG TWRNRYRKRF HGSSNGLKWA
DSGQNTAEMA KKSTIIHIDL DCFFVSVVIK NRLELHDKPV AVCHSDNPKG TAEISSANYP
ARAYGVKAGM FVRHAKDLCP QLVIVPYNFE AYEEVADQFY DILHRHCRKV QALSCDEAFL
DVSDLSDVET EVLASTIRNE ILETTGCSAS AGIGGTMLMA RLATRVAKPA GQLYISAEKV
EEFLDQLPVG TLPGVGSVLK EKLVKQNIQT CGQLRLISKD SLQKDFGVKT GEMLWSYSRG
LDLRSVTAVQ ESKSIGAEVN WGVRFRDQQD VFILVQHFLQ CLCKEVSLRL QGCEMIGRTF
TLKIKKRKKD AEEPTKYMGC GDCDNLSRSI TVPAATDDIE VLQRISKKLF GSFCLDVKEV
RGVGLQVSKL DSADPSNKGS RTLKSWLSSA PAVVQIEQDD NVFAAKVREN SDCNRPVTGG
VSRLRESNSE ESSIQSGDTN SSLPPMCYLD MEVLENLPPE LLSELDGTYG GKLFELIEKK
RGKRRINCNS PHVSLDGTAA SIKELKSLSV KIHGLSTSGE KEYKEPYVPH PSIARTSNQH
TIEMTDLLPS SLSQVDVSVL QELPEELRAD VLGAFPSHRR QQSSSDVPKE TCKKQDEEPI
DLKGTENEIG LSFSSLWFGN PPLWTEKFKV SGNCTMEKLS AIYFKVAQSR PMLSLVLQHA
ISEMSSFPDA ASASDLDKAI YDVCELLKQY INLKVGGDIE EIYLCFRLLK RLAARSQLFL
QVYEILSPFI QASISEHYGG SLSIP
