ID1_HUMAN
ID ID1_HUMAN Reviewed; 155 AA.
AC P41134; A8K537; E1P5L4; O00651; O00652; Q16371; Q16377; Q5TE66; Q5TE67;
AC Q969Z7; Q9H0Z5; Q9H109;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=DNA-binding protein inhibitor ID-1;
DE AltName: Full=Class B basic helix-loop-helix protein 24;
DE Short=bHLHb24;
DE AltName: Full=Inhibitor of DNA binding 1;
DE AltName: Full=Inhibitor of differentiation 1;
GN Name=ID1; Synonyms=BHLHB24, ID;
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 ID-A).
RC TISSUE=Placenta;
RX PubMed=8086456; DOI=10.1016/0167-4781(94)90261-5;
RA Deed R.W., Jasiok M., Norton J.D.;
RT "Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1
RT protein: identification of functionally conserved residues common to Id
RT proteins.";
RL Biochim. Biophys. Acta 1219:160-162(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ID-A AND ID-B).
RC TISSUE=Lung;
RX PubMed=8294468; DOI=10.1016/s0021-9258(17)42146-6;
RA Hara E., Yamaguchi T., Nojima H., Ide T., Campisi J., Okayama H., Oda K.;
RT "Id-related genes encoding helix-loop-helix proteins are required for G1
RT progression and are repressed in senescent human fibroblasts.";
RL J. Biol. Chem. 269:2139-2145(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ID-A AND ID-B).
RX PubMed=7637581; DOI=10.1016/0169-328x(95)00017-m;
RA Zhu W., Dahmen J., Bulfone A., Rigolet M., Hernandez M.-C., Kuo W.L.,
RA Puelles L., Rubenstein J.L.R., Israel M.A.;
RT "Id gene expression during development and molecular cloning of the human
RT Id-1 gene.";
RL Brain Res. Mol. Brain Res. 30:312-326(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=9070860; DOI=10.1006/bbrc.1997.6152;
RA Nehlin J.O., Hara E., Kuo W.L., Collins C., Campisi J.;
RT "Genomic organization, sequence, and chromosomal localization of the human
RT helix-loop-helix Id1 gene.";
RL Biochem. Biophys. Res. Commun. 231:628-634(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ID-A).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ID-A).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ID-A).
RC TISSUE=Ovary, and Skin;
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 [10]
RP INTERACTION WITH CLOCK AND ARNTL.
RX PubMed=20861012; DOI=10.1074/jbc.m110.175182;
RA Ward S.M., Fernando S.J., Hou T.Y., Duffield G.E.;
RT "The transcriptional repressor ID2 can interact with the canonical clock
RT components CLOCK and BMAL1 and mediate inhibitory effects on mPer1
RT expression.";
RL J. Biol. Chem. 285:38987-39000(2010).
CC -!- FUNCTION: Transcriptional regulator (lacking a basic DNA binding
CC domain) which negatively regulates the basic helix-loop-helix (bHLH)
CC transcription factors by forming heterodimers and inhibiting their DNA
CC binding and transcriptional activity. Implicated in regulating a
CC variety of cellular processes, including cellular growth, senescence,
CC differentiation, apoptosis, angiogenesis, and neoplastic
CC transformation. Inhibits skeletal muscle and cardiac myocyte
CC differentiation. Regulates the circadian clock by repressing the
CC transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with other HLH proteins. Interacts with COPS5,
CC IFI204, GATA4 and NKX2-5 (By similarity). Interacts with CLOCK and
CC ARNTL/BMAL1. {ECO:0000250, ECO:0000269|PubMed:20861012}.
CC -!- INTERACTION:
CC P41134; Q9NQ33: ASCL3; NbExp=3; IntAct=EBI-1215527, EBI-12108222;
CC P41134; O14936: CASK; NbExp=3; IntAct=EBI-1215527, EBI-1215506;
CC P41134; Q03135: CAV1; NbExp=6; IntAct=EBI-1215527, EBI-603614;
CC P41134; P28329-3: CHAT; NbExp=3; IntAct=EBI-1215527, EBI-25837549;
CC P41134; P22607: FGFR3; NbExp=3; IntAct=EBI-1215527, EBI-348399;
CC P41134; P06396: GSN; NbExp=3; IntAct=EBI-1215527, EBI-351506;
CC P41134; A6NI15: MSGN1; NbExp=5; IntAct=EBI-1215527, EBI-11991020;
CC P41134; P13349: MYF5; NbExp=5; IntAct=EBI-1215527, EBI-17491620;
CC P41134; P15173: MYOG; NbExp=4; IntAct=EBI-1215527, EBI-3906629;
CC P41134; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1215527, EBI-5235340;
CC P41134; Q99081: TCF12; NbExp=3; IntAct=EBI-1215527, EBI-722877;
CC P41134; Q99081-3: TCF12; NbExp=3; IntAct=EBI-1215527, EBI-11952764;
CC P41134; P15923-3: TCF3; NbExp=3; IntAct=EBI-1215527, EBI-12000326;
CC P41134; P15884: TCF4; NbExp=3; IntAct=EBI-1215527, EBI-533224;
CC P41134; P15884-3: TCF4; NbExp=3; IntAct=EBI-1215527, EBI-13636688;
CC P41134; Q9Y649; NbExp=3; IntAct=EBI-1215527, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=ID-A;
CC IsoId=P41134-1; Sequence=Displayed;
CC Name=ID-B;
CC IsoId=P41134-2; Sequence=VSP_002108;
CC -!- DEVELOPMENTAL STAGE: Expression correlates with proliferation in some
CC types of cells.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ID1ID40914ch20q11.html";
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DR EMBL; X77956; CAA54920.1; -; mRNA.
DR EMBL; D13889; BAA02988.1; -; mRNA.
DR EMBL; D13890; BAA02989.1; -; mRNA.
DR EMBL; S78986; AAB35037.1; -; mRNA.
DR EMBL; S78825; AAB35038.1; -; mRNA.
DR EMBL; U57645; AAC13882.1; -; Genomic_DNA.
DR EMBL; U57645; AAC13883.1; -; Genomic_DNA.
DR EMBL; BT007443; AAP36111.1; -; mRNA.
DR EMBL; AK291152; BAF83841.1; -; mRNA.
DR EMBL; AL110115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76432.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76434.1; -; Genomic_DNA.
DR EMBL; BC000613; AAH00613.1; -; mRNA.
DR EMBL; BC012420; AAH12420.1; -; mRNA.
DR CCDS; CCDS13185.1; -. [P41134-1]
DR CCDS; CCDS13186.1; -. [P41134-2]
DR PIR; A49727; A49727.
DR PIR; B49727; B49727.
DR PIR; JC5395; JC5395.
DR PIR; JC5396; JC5396.
DR PIR; S47524; S47524.
DR RefSeq; NP_002156.2; NM_002165.3. [P41134-1]
DR RefSeq; NP_851998.1; NM_181353.2. [P41134-2]
DR AlphaFoldDB; P41134; -.
DR SMR; P41134; -.
DR BioGRID; 109623; 57.
DR DIP; DIP-38112N; -.
DR IntAct; P41134; 41.
DR MINT; P41134; -.
DR STRING; 9606.ENSP00000365280; -.
DR ChEMBL; CHEMBL1075116; -.
DR iPTMnet; P41134; -.
DR PhosphoSitePlus; P41134; -.
DR BioMuta; ID1; -.
DR DMDM; 21264450; -.
DR EPD; P41134; -.
DR jPOST; P41134; -.
DR MassIVE; P41134; -.
DR MaxQB; P41134; -.
DR PaxDb; P41134; -.
DR PeptideAtlas; P41134; -.
DR PRIDE; P41134; -.
DR ProteomicsDB; 55400; -. [P41134-1]
DR ProteomicsDB; 55401; -. [P41134-2]
DR Antibodypedia; 25205; 396 antibodies from 37 providers.
DR DNASU; 3397; -.
DR Ensembl; ENST00000376105.4; ENSP00000365273.3; ENSG00000125968.9. [P41134-2]
DR Ensembl; ENST00000376112.4; ENSP00000365280.3; ENSG00000125968.9. [P41134-1]
DR GeneID; 3397; -.
DR KEGG; hsa:3397; -.
DR MANE-Select; ENST00000376112.4; ENSP00000365280.3; NM_002165.4; NP_002156.2.
DR UCSC; uc002wwg.3; human. [P41134-1]
DR CTD; 3397; -.
DR DisGeNET; 3397; -.
DR GeneCards; ID1; -.
DR HGNC; HGNC:5360; ID1.
DR HPA; ENSG00000125968; Low tissue specificity.
DR MIM; 600349; gene.
DR neXtProt; NX_P41134; -.
DR OpenTargets; ENSG00000125968; -.
DR PharmGKB; PA29608; -.
DR VEuPathDB; HostDB:ENSG00000125968; -.
DR eggNOG; ENOG502RZP5; Eukaryota.
DR GeneTree; ENSGT00940000161109; -.
DR HOGENOM; CLU_116790_0_0_1; -.
DR InParanoid; P41134; -.
DR OMA; QMNVFLQ; -.
DR OrthoDB; 1624054at2759; -.
DR PhylomeDB; P41134; -.
DR TreeFam; TF326217; -.
DR PathwayCommons; P41134; -.
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; P41134; -.
DR SIGNOR; P41134; -.
DR BioGRID-ORCS; 3397; 29 hits in 1102 CRISPR screens.
DR ChiTaRS; ID1; human.
DR GeneWiki; ID1; -.
DR GenomeRNAi; 3397; -.
DR Pharos; P41134; Tbio.
DR PRO; PR:P41134; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P41134; protein.
DR Bgee; ENSG00000125968; Expressed in seminal vesicle and 194 other tissues.
DR Genevisible; P41134; HS.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0070628; F:proteasome binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:ARUK-UCL.
DR GO; GO:0001525; P:angiogenesis; TAS:BHF-UCL.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; TAS:BHF-UCL.
DR GO; GO:0048514; P:blood vessel morphogenesis; TAS:BHF-UCL.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0036164; P:cell-abiotic substrate adhesion; IEA:Ensembl.
DR GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:ARUK-UCL.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; TAS:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:GDB.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1901342; P:regulation of vasculature development; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:BHF-UCL.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR026052; DNA-bd_prot-inh.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR11723; PTHR11723; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cytoplasm; Developmental protein;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..155
FT /note="DNA-binding protein inhibitor ID-1"
FT /id="PRO_0000127236"
FT DOMAIN 53..105
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT MOTIF 98..111
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT VAR_SEQ 143..155
FT /note="AACVPADDRILCR -> VRSRSDH (in isoform ID-B)"
FT /evidence="ECO:0000303|PubMed:7637581,
FT ECO:0000303|PubMed:8294468"
FT /id="VSP_002108"
FT VARIANT 63
FT /note="N -> D (in dbSNP:rs1802548)"
FT /id="VAR_049544"
FT CONFLICT 16
FT /note="S -> T (in Ref. 2; BAA02988/BAA02989)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="Missing (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 16133 MW; 480287384B667161 CRC64;
MKVASGSTAT AAAGPSCALK AGKTASGAGE VVRCLSEQSV AISRCAGGAG ARLPALLDEQ
QVNVLLYDMN GCYSRLKELV PTLPQNRKVS KVEILQHVID YIRDLQLELN SESEVGTPGG
RGLPVRAPLS TLNGEISALT AEAACVPADD RILCR
