BABA2_MOUSE
ID BABA2_MOUSE Reviewed; 383 AA.
AC Q8K3W0; Q497G6; Q6P8Z2; Q8BKU1; Q8CJ13; Q8JZP0; Q8K3V9; Q8VHN1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=BRISC and BRCA1-A complex member 2;
DE AltName: Full=BRCA1-A complex subunit BRE;
DE AltName: Full=BRCA1/BRCA2-containing complex subunit 45;
DE AltName: Full=Brain and reproductive organ-expressed protein;
GN Name=Babam2; Synonyms=Bre {ECO:0000312|MGI:MGI:1333875};
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] {ECO:0000305, ECO:0000312|EMBL:AAM92774.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAM92774.1}, and C57BL/6 X CBA/N;
RC TISSUE=Heart {ECO:0000312|EMBL:AAM92774.1};
RX PubMed=14565866; DOI=10.1089/10445490360708900;
RA Ching A.K.K., Li Q., Lim P.L., Chan J.Y.-H., Chui Y.L.;
RT "Expression of a conserved mouse stress-modulating gene, Bre: comparison
RT with the human ortholog.";
RL DNA Cell Biol. 22:497-504(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC34385.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC34385.1}, and
RC NOD {ECO:0000312|EMBL:BAE33900.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC34385.1},
RC Medulla oblongata {ECO:0000312|EMBL:BAC38108.1}, and
RC Spleen {ECO:0000312|EMBL:BAE33900.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAH61000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Kidney {ECO:0000312|EMBL:AAH61000.1}, and Lung;
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 [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH TNFRSF1A.
RX PubMed=9737713; DOI=10.1096/fasebj.12.12.1101;
RA Gu C., Castellino A., Chan J.Y.-H., Chao M.V.;
RT "BRE: a modulator of TNF-alpha action.";
RL FASEB J. 12:1101-1108(1998).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=11676476; DOI=10.1006/bbrc.2001.5801;
RA Ching A.K.K., Li P.S., Li Q., Chan B.C.L., Chan J.Y.-H., Lim P.L.,
RA Pang J.C.S., Chui Y.L.;
RT "Expression of human BRE in multiple isoforms.";
RL Biochem. Biophys. Res. Commun. 288:535-545(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically
CC recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA
CC lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites
CC of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also
CC possesses deubiquitinase activity that specifically removes 'Lys-63'-
CC linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it
CC acts as an adapter that bridges the interaction between BABAM1/NBA1 and
CC the rest of the complex, thereby being required for the complex
CC integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-
CC BARD1 heterodimer. Probably also plays a role as a component of the
CC BRISC complex, a multiprotein complex that specifically cleaves 'Lys-
CC 63'-linked ubiquitin (By similarity). May regulate TNF-alpha signaling
CC through its interactions with TNFRSF1A. {ECO:0000250,
CC ECO:0000269|PubMed:9737713}.
CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically
CC recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA
CC lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites
CC of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also
CC possesses deubiquitinase activity that specifically removes 'Lys-63'-
CC linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it
CC acts as an adapter that bridges the interaction between BABAM1/NBA1 and
CC the rest of the complex, thereby being required for the complex
CC integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-
CC BARD1 heterodimer. Component of the BRISC complex, a multiprotein
CC complex that specifically cleaves 'Lys-63'-linked ubiquitin in various
CC substrates. Within the BRISC complex, acts as an adapter that bridges
CC the interaction between BABAM1/NBA1 and the rest of the complex,
CC thereby being required for the complex integrity. The BRISC complex is
CC required for normal mitotic spindle assembly and microtubule attachment
CC to kinetochores via its role in deubiquitinating NUMA1. The BRISC
CC complex plays a role in interferon signaling via its role in the
CC deubiquitination of the interferon receptor IFNAR1; deubiquitination
CC increases IFNAR1 activity by enhancing its stability and cell surface
CC expression. Down-regulates the response to bacterial lipopolysaccharide
CC (LPS) via its role in IFNAR1 deubiquitination. May play a role in
CC homeostasis or cellular differentiation in cells of neural, epithelial
CC and germline origins (By similarity). May also act as a death receptor-
CC associated anti-apoptotic protein, which inhibits the mitochondrial
CC apoptotic pathway. May regulate TNF-alpha signaling through its
CC interactions with TNFRSF1A; however these effects may be indirect
CC (PubMed:9737713). {ECO:0000250|UniProtKB:Q9NXR7,
CC ECO:0000305|PubMed:9737713}.
CC -!- SUBUNIT: Component of the ARISC complex, at least composed of
CC UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Component
CC of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80,
CC ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the BRCA1-A complex,
CC interacts directly with ABRAXAS1, BRCC3/BRCC36 and BABAM1/NBA1. Binds
CC polyubiquitin. Component of the BRISC complex, at least composed of
CC ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Identified in a complex
CC with SHMT2 and the other subunits of the BRISC complex. Component of
CC the BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1,
CC BRCA2, BARD1, BRCC3/BRCC36 and RAD51. BRCC is a ubiquitin E3 ligase
CC complex that enhances cellular survival following DNA damage. May
CC interact with FAS and TNFRSF1A (PubMed:9737713).
CC {ECO:0000250|UniProtKB:Q9NXR7, ECO:0000305|PubMed:9737713}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NXR7}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NXR7}. Note=Localizes at sites of DNA damage
CC at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q9NXR7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms may exist. {ECO:0000305};
CC Name=2 {ECO:0000269|PubMed:14565866};
CC IsoId=Q8K3W0-2; Sequence=Displayed;
CC Name=1 {ECO:0000269|PubMed:14565866}; Synonyms=I
CC {ECO:0000269|PubMed:14565866};
CC IsoId=Q8K3W0-1; Sequence=VSP_051953;
CC Name=3; Synonyms=II, II3+;
CC IsoId=Q8K3W0-4; Sequence=VSP_051952;
CC Name=4; Synonyms=IV;
CC IsoId=Q8K3W0-5; Sequence=VSP_037263;
CC Name=5; Synonyms=III;
CC IsoId=Q8K3W0-6; Sequence=VSP_037262;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC testis, germinal center B-cells and various mouse cell lines.
CC {ECO:0000269|PubMed:11676476, ECO:0000269|PubMed:14565866}.
CC -!- DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-like)
CC regions. These regions lack the critical Cys residues required for
CC ubiquitination but retain the ability to bind ubiquitin (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-like)
CC regions. These regions lack the critical Cys residues required for
CC ubiquitination but retain the ability to bind ubiquitin.
CC {ECO:0000250|UniProtKB:Q9NXR7}.
CC -!- SIMILARITY: Belongs to the BABAM2 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34385.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AF440752; AAL40809.1; -; mRNA.
DR EMBL; AF527952; AAM92774.1; -; mRNA.
DR EMBL; AF527953; AAM92775.1; -; mRNA.
DR EMBL; AF527954; AAM92776.1; -; mRNA.
DR EMBL; AF527955; AAM92777.1; -; mRNA.
DR EMBL; AF538925; AAN15148.1; -; mRNA.
DR EMBL; AK050695; BAC34385.1; ALT_SEQ; mRNA.
DR EMBL; AK080991; BAC38108.1; -; mRNA.
DR EMBL; AK156929; BAE33900.1; -; mRNA.
DR EMBL; BC061000; AAH61000.1; -; mRNA.
DR EMBL; BC100565; AAI00566.1; -; mRNA.
DR CCDS; CCDS19188.1; -. [Q8K3W0-2]
DR CCDS; CCDS19189.1; -. [Q8K3W0-1]
DR CCDS; CCDS39058.1; -. [Q8K3W0-5]
DR CCDS; CCDS39059.1; -. [Q8K3W0-4]
DR CCDS; CCDS51461.1; -. [Q8K3W0-6]
DR RefSeq; NP_653124.1; NM_144541.1. [Q8K3W0-2]
DR RefSeq; NP_851796.1; NM_181279.1. [Q8K3W0-1]
DR RefSeq; NP_851797.1; NM_181280.1. [Q8K3W0-5]
DR RefSeq; NP_851798.1; NM_181281.1. [Q8K3W0-6]
DR RefSeq; NP_851799.1; NM_181282.1. [Q8K3W0-4]
DR PDB; 6GVW; X-ray; 3.75 A; C/H=1-383.
DR PDBsum; 6GVW; -.
DR AlphaFoldDB; Q8K3W0; -.
DR SMR; Q8K3W0; -.
DR BioGRID; 223733; 16.
DR ComplexPortal; CPX-4702; BRCA1-A complex.
DR ComplexPortal; CPX-972; BRCC ubiquitin ligase complex.
DR iPTMnet; Q8K3W0; -.
DR PhosphoSitePlus; Q8K3W0; -.
DR SwissPalm; Q8K3W0; -.
DR EPD; Q8K3W0; -.
DR jPOST; Q8K3W0; -.
DR MaxQB; Q8K3W0; -.
DR PeptideAtlas; Q8K3W0; -.
DR PRIDE; Q8K3W0; -.
DR ProteomicsDB; 273528; -. [Q8K3W0-2]
DR ProteomicsDB; 273529; -. [Q8K3W0-1]
DR ProteomicsDB; 273530; -. [Q8K3W0-4]
DR ProteomicsDB; 273531; -. [Q8K3W0-5]
DR ProteomicsDB; 273532; -. [Q8K3W0-6]
DR Antibodypedia; 13903; 260 antibodies from 35 providers.
DR Ensembl; ENSMUST00000063813; ENSMUSP00000069133; ENSMUSG00000052139. [Q8K3W0-1]
DR Ensembl; ENSMUST00000071531; ENSMUSP00000071462; ENSMUSG00000052139. [Q8K3W0-5]
DR Ensembl; ENSMUST00000114507; ENSMUSP00000110152; ENSMUSG00000052139. [Q8K3W0-6]
DR Ensembl; ENSMUST00000131995; ENSMUSP00000128351; ENSMUSG00000052139. [Q8K3W0-4]
DR Ensembl; ENSMUST00000201352; ENSMUSP00000144205; ENSMUSG00000052139. [Q8K3W0-2]
DR GeneID; 107976; -.
DR KEGG; mmu:107976; -.
DR UCSC; uc008wza.1; mouse. [Q8K3W0-2]
DR UCSC; uc008wzb.1; mouse. [Q8K3W0-1]
DR UCSC; uc008wzc.1; mouse. [Q8K3W0-5]
DR UCSC; uc008wze.1; mouse. [Q8K3W0-6]
DR CTD; 9577; -.
DR MGI; MGI:1333875; Babam2.
DR VEuPathDB; HostDB:ENSMUSG00000052139; -.
DR GeneTree; ENSGT00390000004208; -.
DR HOGENOM; CLU_1133268_0_0_1; -.
DR InParanoid; Q8K3W0; -.
DR OMA; KPTEARF; -.
DR OrthoDB; 831092at2759; -.
DR PhylomeDB; Q8K3W0; -.
DR TreeFam; TF328507; -.
DR Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 107976; 9 hits in 111 CRISPR screens.
DR ChiTaRS; Bre; mouse.
DR PRO; PR:Q8K3W0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K3W0; protein.
DR Bgee; ENSMUSG00000052139; Expressed in lens of camera-type eye and 254 other tissues.
DR ExpressionAtlas; Q8K3W0; baseline and differential.
DR Genevisible; Q8K3W0; MM.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR GO; GO:0070552; C:BRISC complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; IC:ComplexPortal.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IC:ComplexPortal.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IC:ComplexPortal.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IC:ComplexPortal.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR010358; BRE.
DR PANTHER; PTHR15189; PTHR15189; 1.
DR Pfam; PF06113; BRE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell cycle;
KW Cell division; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..383
FT /note="BRISC and BRCA1-A complex member 2"
FT /id="PRO_0000224190"
FT REGION 30..147
FT /note="UEV-like 1"
FT REGION 275..364
FT /note="UEV-like 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR7"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR7"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14565866"
FT /id="VSP_051952"
FT VAR_SEQ 1..69
FT /note="MSPEIALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPN
FT CDRFKLHIPYAGETLKW -> MCACR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14565866"
FT /id="VSP_037262"
FT VAR_SEQ 1..43
FT /note="MSPEIALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSG -> MCACN
FT EWYGVPDLEKASYLWRKKENHLPLEKGQN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14565866"
FT /id="VSP_037263"
FT VAR_SEQ 27..43
FT /note="VGLDATNCLRITDLKSG -> IHEKGPSQKLSFKSCSYHLPMCACNEWYGVP
FT DLEKASYLWRKKENHLPLEKGQN (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14565866"
FT /id="VSP_051953"
FT CONFLICT 105
FT /note="W -> R (in Ref. 3; AAH61000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 43545 MW; 7BABA837A8AF82E6 CRC64;
MSPEIALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG PNCDRFKLHI
PYAGETLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALH NLASWNPSNP ECLLLVVKEL
VQQYHQFQCG RLRESSRLMF EYQTLLEEPQ YGENMEIYAG KKNNWTGEFS ARFLLKLPVD
FSNIPTYLLK DVNEDPGEDV ALLSVSFEDT EATQVYPKLY LSPRIEHALG GSSALHIPAF
PGGGCLIDYV PQVCHLLTNK VQYVIQGYHK RREYIAAFLS HFGTGVVEYD AEGFTKLTLL
LMWKDFCFLV HIDLPLFFPR DQPTLTFQSV YHFTNSGQLY SQAQKNYPYS PRWDGNEMAK
RAKAYFKTFV PQFQEAAFAN GKL
