NIBA1_HUMAN
ID NIBA1_HUMAN Reviewed; 928 AA.
AC Q9BZQ8; Q2TTR2; Q5TEM8; Q8TEI5; Q9H593; Q9H9Y8; Q9HCB9;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein Niban 1 {ECO:0000305};
DE AltName: Full=Cell growth-inhibiting gene 39 protein;
DE AltName: Full=Protein FAM129A;
GN Name=NIBAN1 {ECO:0000312|HGNC:HGNC:16784};
GN Synonyms=C1orf24, FAM129A, NIBAN; ORFNames=GIG39;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Renal cell carcinoma;
RX PubMed=11011112; DOI=10.1111/j.1349-7006.2000.tb01027.x;
RA Majima S., Kajino K., Fukuda T., Otsuka F., Hino O.;
RT "A novel gene 'Niban' upregulated in renal carcinogenesis: cloning by the
RT cDNA-amplified fragment length polymorphism approach.";
RL Jpn. J. Cancer Res. 91:869-874(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA Carpten J.D.;
RT "Cloning and characterization of 13 novel transcripts and the human RGS8
RT gene from the 1q25 region encompassing the hereditary prostate cancer
RT (HPC1) locus.";
RL Genomics 73:211-222(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human cell growth inhibiting gene.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leukocyte;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 522-928, AND VARIANT ASN-692.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16949643; DOI=10.1016/j.humpath.2006.06.022;
RA Matsumoto F., Fujii H., Abe M., Kajino K., Kobayashi T., Matsumoto T.,
RA Ikeda K., Hino O.;
RT "A novel tumor marker, Niban, is expressed in subsets of thyroid tumors and
RT Hashimoto's thyroiditis.";
RL Hum. Pathol. 37:1592-1600(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; SER-596; SER-602;
RP SER-646 AND SER-926, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602 AND SER-926, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-602 AND SER-708, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
CC -!- FUNCTION: Regulates phosphorylation of a number of proteins involved in
CC translation regulation including EIF2A, EIF4EBP1 and RPS6KB1. May be
CC involved in the endoplasmic reticulum stress response (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BZQ8; P31749: AKT1; NbExp=2; IntAct=EBI-6916466, EBI-296087;
CC Q9BZQ8; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-6916466, EBI-742054;
CC Q9BZQ8; Q14192: FHL2; NbExp=6; IntAct=EBI-6916466, EBI-701903;
CC Q9BZQ8; P06748: NPM1; NbExp=7; IntAct=EBI-6916466, EBI-78579;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16949643}. Membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in various types of thyroid tumor such as
CC papillary thyroid carcinomas and oxyphilic thyroid tumors but not in
CC normal thyroid tissue (at protein level). Strongly expressed in heart,
CC skeletal muscle, pancreas, white blood cells and prostate with moderate
CC expression in colon and spleen. Expressed in renal carcinoma cells but
CC not in normal kidney. {ECO:0000269|PubMed:11011112,
CC ECO:0000269|PubMed:16949643}.
CC -!- MISCELLANEOUS: 'Niban' means 'second' in Japanese.
CC -!- SIMILARITY: Belongs to the Niban family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB17230.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB050477; BAB17230.1; ALT_INIT; mRNA.
DR EMBL; AF288391; AAG60611.1; -; mRNA.
DR EMBL; AK022527; BAB14079.1; -; mRNA.
DR EMBL; AY550972; AAT52218.1; -; mRNA.
DR EMBL; AL096819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030531; AAH30531.1; -; mRNA.
DR EMBL; AK074139; BAB84965.1; -; mRNA.
DR CCDS; CCDS1364.1; -.
DR RefSeq; NP_443198.1; NM_052966.3.
DR AlphaFoldDB; Q9BZQ8; -.
DR SMR; Q9BZQ8; -.
DR BioGRID; 125515; 17.
DR IntAct; Q9BZQ8; 4.
DR MINT; Q9BZQ8; -.
DR STRING; 9606.ENSP00000356481; -.
DR iPTMnet; Q9BZQ8; -.
DR MetOSite; Q9BZQ8; -.
DR PhosphoSitePlus; Q9BZQ8; -.
DR BioMuta; FAM129A; -.
DR DMDM; 22256936; -.
DR CPTAC; CPTAC-1623; -.
DR EPD; Q9BZQ8; -.
DR jPOST; Q9BZQ8; -.
DR MassIVE; Q9BZQ8; -.
DR MaxQB; Q9BZQ8; -.
DR PaxDb; Q9BZQ8; -.
DR PeptideAtlas; Q9BZQ8; -.
DR PRIDE; Q9BZQ8; -.
DR ProteomicsDB; 79893; -.
DR Antibodypedia; 34451; 201 antibodies from 31 providers.
DR DNASU; 116496; -.
DR Ensembl; ENST00000367511.4; ENSP00000356481.3; ENSG00000135842.17.
DR GeneID; 116496; -.
DR KEGG; hsa:116496; -.
DR MANE-Select; ENST00000367511.4; ENSP00000356481.3; NM_052966.4; NP_443198.1.
DR UCSC; uc001gra.5; human.
DR CTD; 116496; -.
DR DisGeNET; 116496; -.
DR GeneCards; NIBAN1; -.
DR HGNC; HGNC:16784; NIBAN1.
DR HPA; ENSG00000135842; Tissue enhanced (heart).
DR MIM; 619294; gene.
DR neXtProt; NX_Q9BZQ8; -.
DR OpenTargets; ENSG00000135842; -.
DR PharmGKB; PA162385951; -.
DR VEuPathDB; HostDB:ENSG00000135842; -.
DR eggNOG; ENOG502QVNR; Eukaryota.
DR GeneTree; ENSGT00940000154149; -.
DR HOGENOM; CLU_009718_0_1_1; -.
DR InParanoid; Q9BZQ8; -.
DR OMA; PKCRILP; -.
DR OrthoDB; 164866at2759; -.
DR PhylomeDB; Q9BZQ8; -.
DR TreeFam; TF333351; -.
DR PathwayCommons; Q9BZQ8; -.
DR SignaLink; Q9BZQ8; -.
DR SIGNOR; Q9BZQ8; -.
DR BioGRID-ORCS; 116496; 12 hits in 1082 CRISPR screens.
DR ChiTaRS; FAM129A; human.
DR GeneWiki; FAM129A; -.
DR GenomeRNAi; 116496; -.
DR Pharos; Q9BZQ8; Tbio.
DR PRO; PR:Q9BZQ8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BZQ8; protein.
DR Bgee; ENSG00000135842; Expressed in blood vessel layer and 195 other tissues.
DR ExpressionAtlas; Q9BZQ8; baseline and differential.
DR Genevisible; Q9BZQ8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR InterPro; IPR026088; Niban-like.
DR PANTHER; PTHR14392; PTHR14392; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome; Stress response; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25807930"
FT CHAIN 2..928
FT /note="Protein Niban 1"
FT /id="PRO_0000213120"
FT REGION 580..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25807930"
FT VARIANT 633
FT /note="S -> L (in dbSNP:rs12750174)"
FT /id="VAR_053533"
FT VARIANT 692
FT /note="D -> N (in dbSNP:rs35704242)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_053534"
FT VARIANT 720
FT /note="V -> M (in dbSNP:rs17313374)"
FT /id="VAR_053535"
FT VARIANT 830
FT /note="G -> S (in dbSNP:rs35601690)"
FT /id="VAR_053536"
FT CONFLICT 27
FT /note="N -> D (in Ref. 4; AAT52218)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="E -> G (in Ref. 3; BAB14079)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="D -> E (in Ref. 3; BAB14079)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="L -> P (in Ref. 7; BAB84965)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="V -> D (in Ref. 3; BAB14079)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="E -> D (in Ref. 3; BAB14079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 103135 MW; 93717F41336488FE CRC64;
MGGSASSQLD EGKCAYIRGK TEAAIKNFSP YYSRQYSVAF CNHVRTEVEQ QRDLTSQFLK
TKPPLAPGTI LYEAELSQFS EDIKKWKERY VVVKNDYAVE SYENKEAYQR GAAPKCRILP
AGGKVLTSED EYNLLSDRHF PDPLASSEKE NTQPFVVLPK EFPVYLWQPF FRHGYFCFHE
AADQKRFSAL LSDCVRHLNH DYMKQMTFEA QAFLEAVQFF RQEKGHYGSW EMITGDEIQI
LSNLVMEELL PTLQTDLLPK MKGKKNDRKR TWLGLLEEAY TLVQHQVSEG LSALKEECRA
LTKGLEGTIR SDMDQIVNSK NYLIGKIKAM VAQPAEKSCL ESVQPFLASI LEELMGPVSS
GFSEVRVLFE KEVNEVSQNF QTTKDSVQLK EHLDRLMNLP LHSVKMEPCY TKVNLLHERL
QDLKSRFRFP HIDLVVQRTQ NYMQELMENA VFTFEQLLSP HLQGEASKTA VAIEKVKLRV
LKQYDYDSST IRKKIFQEAL VQITLPTVQK ALASTCKPEL QKYEQFIFAD HTNMIHVENV
YEEILHQILL DETLKVIKEA AILKKHNLFE DNMALPSESV SSLTDLKPPT GSNQASPARR
ASAILPGVLG SETLSNEVFQ ESEEEKQPEV PSSLAKGESL SLPGPSPPPD GTEQVIISRV
DDPVVNPVAT EDTAGLPGTC SSELEFGGTL EDEEPAQEEP EPITASGSLK ALRKLLTASV
EVPVDSAPVM EEDTNGESHV PQENEEEEEK EPSQAAAIHP DNCEESEVSE REAQPPCPEA
HGEELGGFPE VGSPASPPAS GGLTEEPLGP MEGELPGEAC TLTAHEGRGG KCTEEGDASQ
QEGCTLGSDP ICLSESQVSE EQEEMGGQSS AAQATASVNA EEIKVARIHE CQWVVEDAPN
PDVLLSHKDD VKEGEGGQES FPELPSEE
