TRIP4_MOUSE
ID TRIP4_MOUSE Reviewed; 581 AA.
AC Q9QXN3; E9QK64; Q8CAD5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Activating signal cointegrator 1 {ECO:0000303|PubMed:12077347};
DE Short=ASC-1 {ECO:0000303|PubMed:12077347};
DE AltName: Full=Thyroid receptor-interacting protein 4 {ECO:0000305};
DE Short=TR-interacting protein 4 {ECO:0000305};
DE Short=TRIP-4 {ECO:0000305};
GN Name=Trip4 {ECO:0000312|MGI:MGI:1928469};
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 1), AND IDENTIFICATION OF THE ASC-1
RP COMPLEX.
RC TISSUE=Liver;
RX PubMed=12077347; DOI=10.1128/mcb.22.14.5203-5211.2002;
RA Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y., Lim J.,
RA Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C.;
RT "Novel transcription coactivator complex containing activating signal
RT cointegrator 1.";
RL Mol. Cell. Biol. 22:5203-5211(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=12390891; DOI=10.1095/biolreprod.102.006155;
RA Lee Y.S., Kim H.-J., Lee H.J., Lee J.W., Chun S.-Y., Ko S.-K., Lee K.;
RT "Activating signal cointegrator 1 is highly expressed in murine testicular
RT Leydig cells and enhances the ligand-dependent transactivation of androgen
RT receptor.";
RL Biol. Reprod. 67:1580-1587(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PROTEIN SEQUENCE OF 89-97, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP UFMYLATION.
RX PubMed=21494687; DOI=10.1371/journal.pone.0018517;
RA Lemaire K., Moura R.F., Granvik M., Igoillo-Esteve M., Hohmeier H.E.,
RA Hendrickx N., Newgard C.B., Waelkens E., Cnop M., Schuit F.;
RT "Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect pancreatic
RT beta cells from ER stress-induced apoptosis.";
RL PLoS ONE 6:E18517-E18517(2011).
RN [9]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=26924529; DOI=10.1016/j.ajhg.2016.01.006;
RA Knierim E., Hirata H., Wolf N.I., Morales-Gonzalez S., Schottmann G.,
RA Tanaka Y., Rudnik-Schoeneborn S., Orgeur M., Zerres K., Vogt S.,
RA van Riesen A., Gill E., Seifert F., Zwirner A., Kirschner J., Goebel H.H.,
RA Huebner C., Stricker S., Meierhofer D., Stenzel W., Schuelke M.;
RT "Mutations in subunits of the activating signal cointegrator 1 complex are
RT associated with prenatal spinal muscular atrophy and congenital bone
RT fractures.";
RL Am. J. Hum. Genet. 98:473-489(2016).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27008887; DOI=10.1093/hmg/ddw033;
RA Davignon L., Chauveau C., Julien C., Dill C., Duband-Goulet I., Cabet E.,
RA Buendia B., Lilienbaum A., Rendu J., Minot M.C., Guichet A., Allamand V.,
RA Vadrot N., Faure J., Odent S., Lazaro L., Leroy J.P., Marcorelles P.,
RA Dubourg O., Ferreiro A.;
RT "The transcription coactivator ASC-1 is a regulator of skeletal myogenesis,
RT and its deficiency causes a novel form of congenital muscle disease.";
RL Hum. Mol. Genet. 25:1559-1573(2016).
CC -!- FUNCTION: Transcription coactivator which associates with nuclear
CC receptors, transcriptional coactivators including EP300, CREBBP and
CC NCOA1, and basal transcription factors like TBP and TFIIA to facilitate
CC nuclear receptors-mediated transcription. May thereby play an important
CC role in establishing distinct coactivator complexes under different
CC cellular conditions. Plays a role in thyroid hormone receptor and
CC estrogen receptor transactivation (By similarity). Also involved in
CC androgen receptor transactivation (PubMed:12077347). Plays a pivotal
CC role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a
CC mediator of transrepression between nuclear receptor and either AP1 or
CC NF-kappa-B. May play a role in the development of neuromuscular
CC junction (By similarity). May play a role in late myogenic
CC differentiation (PubMed:27008887). Also functions as part of the RQC
CC trigger (RQT) complex that activates the ribosome quality control (RQC)
CC pathway, a pathway that degrades nascent peptide chains during
CC problematic translation (By similarity). {ECO:0000250|UniProtKB:Q15650,
CC ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:12390891,
CC ECO:0000269|PubMed:27008887}.
CC -!- SUBUNIT: Interacts with the thyroid hormone receptor/TR (via the
CC ligand-binding domain); this interaction requires the presence of
CC thyroid hormone (By similarity). Interacts with the androgen
CC receptor/AR; in an androgen, testosterone and dihydrotestosterone-
CC dependent manner (By similarity). Interacts with ESR1 (estrogen ligand-
CC bound); competes with UFSP2 (By similarity). Interacts with UFSP2;
CC competes with ligand-bound ESR1 (By similarity). Interacts with DDRGK1
CC and UFL1; the interaction with DDRGK1 is direct (By similarity).
CC Interacts with NCOA1 (By similarity). Interacts with EP300 (By
CC similarity). Part of the ASC-1 complex, that contains TRIP4, ASCC1,
CC ASCC2 and ASCC3 (PubMed:12077347). Identified in the RQT (ribosome
CC quality control trigger) complex, that contains ASCC2, ASCC3 and TRIP4
CC (By similarity). Interacts with ASCC2 (By similarity). Interacts with
CC ASCC3 (By similarity). Interacts with NEK6 (By similarity). Interacts
CC with CSRP1 (By similarity). Interacts with ZCCHC4 (By similarity).
CC {ECO:0000250|UniProtKB:Q15650, ECO:0000269|PubMed:12077347}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15650}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15650}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q15650}. Note=Cytoplasmic under conditions of
CC serum deprivation. Colocalizes with NEK6 in the centrosome.
CC {ECO:0000250|UniProtKB:Q15650}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QXN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QXN3-2; Sequence=VSP_011109, VSP_011110;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:12390891). Expressed
CC in the spinal cord, brain, paraspinal ganglia, thyroid, and
CC submandibular glands (PubMed:26924529). Expressed at low level in all
CC the muscles (at protein level) but with higher expression in axial than
CC in limb muscles (PubMed:27008887). {ECO:0000269|PubMed:12390891,
CC ECO:0000269|PubMed:26924529, ECO:0000269|PubMed:27008887}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 17.5-day-old embryos.
CC {ECO:0000269|PubMed:26924529}.
CC -!- DOMAIN: The C4-type zinc finger mediates a competitive interaction with
CC UFSP2 and ligand-bound nuclear receptors. It also mediates interaction
CC with the transcriptional coactivators and the basal transcription
CC machinery. {ECO:0000250|UniProtKB:Q15650}.
CC -!- PTM: Phosphorylated by NEK6. {ECO:0000250}.
CC -!- PTM: Polyufmylated by the UFM1-conjugating system composed of the
CC enzymes UBA5, UFC1 and UFL1. Deufmylated by the protease UFSP2.
CC Ufmylation of TRIP4 is promoted by ligand-bound nuclear receptors that
CC compete with UFSP2 for interaction with TRIP4. Nuclear receptors-
CC induced ufmylation promotes the recruitment of additional
CC transcriptional coactivators like EP300 and NCOA1 and therefore the
CC assembly of a coactivator complex facilitating nuclear receptor-
CC mediated transcription. {ECO:0000250|UniProtKB:Q15650,
CC ECO:0000269|PubMed:21494687}.
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DR EMBL; AF197574; AAF18440.1; -; mRNA.
DR EMBL; AF539614; AAN23117.1; -; mRNA.
DR EMBL; AK039024; BAC30209.1; -; mRNA.
DR EMBL; AC151906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021316; AAH21316.1; -; mRNA.
DR CCDS; CCDS23298.1; -. [Q9QXN3-1]
DR CCDS; CCDS52838.1; -. [Q9QXN3-2]
DR RefSeq; NP_001164378.1; NM_001170907.1. [Q9QXN3-2]
DR RefSeq; NP_062771.2; NM_019797.4. [Q9QXN3-1]
DR RefSeq; XP_006511359.1; XM_006511296.3. [Q9QXN3-1]
DR RefSeq; XP_006511361.1; XM_006511298.3. [Q9QXN3-1]
DR RefSeq; XP_006511362.1; XM_006511299.3.
DR RefSeq; XP_017168981.1; XM_017313492.1. [Q9QXN3-1]
DR RefSeq; XP_017168982.1; XM_017313493.1. [Q9QXN3-2]
DR AlphaFoldDB; Q9QXN3; -.
DR SMR; Q9QXN3; -.
DR BioGRID; 207956; 4.
DR IntAct; Q9QXN3; 3.
DR STRING; 10090.ENSMUSP00000112385; -.
DR iPTMnet; Q9QXN3; -.
DR PhosphoSitePlus; Q9QXN3; -.
DR EPD; Q9QXN3; -.
DR MaxQB; Q9QXN3; -.
DR PaxDb; Q9QXN3; -.
DR PRIDE; Q9QXN3; -.
DR ProteomicsDB; 298312; -. [Q9QXN3-1]
DR ProteomicsDB; 298313; -. [Q9QXN3-2]
DR Antibodypedia; 1761; 296 antibodies from 32 providers.
DR DNASU; 56404; -.
DR Ensembl; ENSMUST00000117083; ENSMUSP00000113949; ENSMUSG00000032386. [Q9QXN3-1]
DR Ensembl; ENSMUST00000119245; ENSMUSP00000112385; ENSMUSG00000032386. [Q9QXN3-1]
DR Ensembl; ENSMUST00000122410; ENSMUSP00000112866; ENSMUSG00000032386. [Q9QXN3-2]
DR Ensembl; ENSMUST00000179395; ENSMUSP00000137304; ENSMUSG00000032386. [Q9QXN3-2]
DR GeneID; 56404; -.
DR KEGG; mmu:56404; -.
DR UCSC; uc009qdz.2; mouse. [Q9QXN3-2]
DR UCSC; uc012gvn.1; mouse. [Q9QXN3-1]
DR CTD; 9325; -.
DR MGI; MGI:1928469; Trip4.
DR VEuPathDB; HostDB:ENSMUSG00000032386; -.
DR eggNOG; KOG2845; Eukaryota.
DR GeneTree; ENSGT00390000005300; -.
DR HOGENOM; CLU_025737_1_0_1; -.
DR InParanoid; Q9QXN3; -.
DR OMA; CVDVTDC; -.
DR OrthoDB; 1132270at2759; -.
DR PhylomeDB; Q9QXN3; -.
DR TreeFam; TF314842; -.
DR BioGRID-ORCS; 56404; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Trip4; mouse.
DR PRO; PR:Q9QXN3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9QXN3; protein.
DR Bgee; ENSMUSG00000032386; Expressed in pineal body and 263 other tissues.
DR ExpressionAtlas; Q9QXN3; baseline and differential.
DR Genevisible; Q9QXN3; MM.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISS:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045661; P:regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR InterPro; IPR007374; ASCH_domain.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR039128; TRIP4-like.
DR InterPro; IPR009349; Znf_C2HC5.
DR PANTHER; PTHR12963; PTHR12963; 1.
DR Pfam; PF04266; ASCH; 1.
DR Pfam; PF06221; zf-C2HC5; 1.
DR SMART; SM01022; ASCH; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15650"
FT CHAIN 2..581
FT /note="Activating signal cointegrator 1"
FT /id="PRO_0000065632"
FT DOMAIN 437..531
FT /note="ASCH"
FT /evidence="ECO:0000255"
FT ZN_FING 167..219
FT /note="C4-type"
FT REGION 100..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..300
FT /note="Mediates interaction with DDRGK1"
FT /evidence="ECO:0000250|UniProtKB:Q15650"
FT REGION 300..400
FT /note="Mediates interaction with UFL1"
FT /evidence="ECO:0000250|UniProtKB:Q15650"
FT REGION 390..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15650"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15650"
FT MOD_RES 289
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1)"
FT /evidence="ECO:0000250|UniProtKB:Q15650"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1)"
FT /evidence="ECO:0000250|UniProtKB:Q15650"
FT VAR_SEQ 526..539
FT /note="FPDISQESDSSFVF -> GNWIPRSIKEQRRG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011109"
FT VAR_SEQ 540..581
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011110"
FT CONFLICT 7
FT /note="A -> G (in Ref. 3; BAC30209)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="S -> P (in Ref. 1; AAF18440, 2; AAN23117 and 5;
FT AAH21316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 66197 MW; 2CAB3512E3CEDDA7 CRC64;
MAVAGAAYRE PLVHWCTQQL QKTFALDVSE EIIQYVLSIE NAEEIREYVT DLLQGNEGKK
GQFIEDLITK WQKNDQEFIS DSFQQCLRKD EILDGQRSVD QLKRSRRKGR NKQEVPAFPE
PDVAVEVKTP LDLAKAQESN NSVKKKTRFV NLYTREGQDK LAVLLPGRHP CDCLGQKHKL
INNCLVCGRI VCEQEGSGPC LFCGSLVCTN EEQDILQRDS NKSQKLLKKL MSGAETSGKV
DVSTKDLLPH QESRMKSGLE KAIKHKEKLL EFDRTSIRRT QVIDDESDYF ASDSNQWLSK
VEREMLQKRE EELRELRHAS RLSKKVTIDF AGRKILEDEN PLAEYHSRLD ETIQAIASGT
LNQSLVTLDR SCEEPLGVLV NPNMYQASPQ WVDNTGSTPQ KKTSLSAGPR LEPSLHQHQL
RIQDQEFQEG FDGGWCLSMH QPWASLLVRG IKRVEGRSWY TPHRGRLWIA ATGKRPSPQE
VSELQATYRL LRGKDVEFPN DYPSGCLLGC VDLIDCLSQK QFQEQFPDIS QESDSSFVFI
CKNPQEMVVK FPIKGNPKIW KLDSKIHQGA KKGLMKQNKA V
