HEBP2_MOUSE
ID HEBP2_MOUSE Reviewed; 205 AA.
AC Q9WU63;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Heme-binding protein 2;
DE AltName: Full=Protein SOUL;
GN Name=Hebp2; Synonyms=Soul;
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].
RX PubMed=10640688; DOI=10.1016/s0169-328x(99)00277-6;
RA Zylka M.J., Reppert S.M.;
RT "Discovery of a putative heme-binding protein family (SOUL/HBP) by two-
RT tissue suppression subtractive hybridization and database searches.";
RL Brain Res. Mol. Brain Res. 74:175-181(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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]
RP FUNCTION AS HEME-BINDING PROTEIN, AND MUTAGENESIS OF HIS-42.
RX PubMed=15518569; DOI=10.1021/bi048742i;
RA Sato E., Sagami I., Uchida T., Sato A., Kitagawa T., Igarashi J.,
RA Shimizu T.;
RT "SOUL in mouse eyes is a new hexameric heme-binding protein with
RT characteristic optical absorption, resonance Raman spectral, and heme-
RT binding properties.";
RL Biochemistry 43:14189-14198(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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: Can promote mitochondrial permeability transition and
CC facilitate necrotic cell death under different types of stress
CC conditions (By similarity). May have low affinity for heme
CC (PubMed:15518569). {ECO:0000250|UniProtKB:Q9Y5Z4}.
CC -!- SUBUNIT: Monomer. Interacts with LRPPRC. May interact with BCL2L1; an
CC interaction with BCL2L1 was observed using a peptide, but not with the
CC full-length protein. The full-length protein would have to undergo a
CC major conformation change for the interaction to occur. Interacts with
CC PDCD6. {ECO:0000250|UniProtKB:Q9Y5Z4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y5Z4}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9Y5Z4}. Note=Mainly localized to
CC the cytoplasm with a much lower abundance in the mitochondrion.
CC {ECO:0000250|UniProtKB:Q9Y5Z4}.
CC -!- DOMAIN: Forms a distorted beta-barrel structure, with two helices that
CC are packed against the outer surface of the barrel.
CC {ECO:0000250|UniProtKB:Q9Y5Z4}.
CC -!- SIMILARITY: Belongs to the HEBP family. {ECO:0000305}.
CC -!- CAUTION: Has been described as heme-binding protein (PubMed:15518569)
CC in mouse, but the human protein does not bind hemin. His-42, a residue
CC essential for heme binding in mouse, is not conserved in all orthologs,
CC or in the heme-binding family member HEBP1.
CC {ECO:0000305|PubMed:15518569}.
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DR EMBL; AF117614; AAD32097.1; -; mRNA.
DR EMBL; AK078130; BAC37141.1; -; mRNA.
DR CCDS; CCDS23711.1; -.
DR RefSeq; NP_062360.1; NM_019487.3.
DR AlphaFoldDB; Q9WU63; -.
DR SMR; Q9WU63; -.
DR BioGRID; 207771; 2.
DR STRING; 10090.ENSMUSP00000020000; -.
DR PhosphoSitePlus; Q9WU63; -.
DR MaxQB; Q9WU63; -.
DR PaxDb; Q9WU63; -.
DR PRIDE; Q9WU63; -.
DR ProteomicsDB; 270897; -.
DR Antibodypedia; 1915; 150 antibodies from 22 providers.
DR DNASU; 56016; -.
DR Ensembl; ENSMUST00000020000; ENSMUSP00000020000; ENSMUSG00000019853.
DR GeneID; 56016; -.
DR KEGG; mmu:56016; -.
DR UCSC; uc007emk.1; mouse.
DR CTD; 23593; -.
DR MGI; MGI:1860084; Hebp2.
DR VEuPathDB; HostDB:ENSMUSG00000019853; -.
DR eggNOG; ENOG502RXJR; Eukaryota.
DR GeneTree; ENSGT00940000160412; -.
DR HOGENOM; CLU_068699_2_1_1; -.
DR InParanoid; Q9WU63; -.
DR OMA; TAYVRTY; -.
DR OrthoDB; 1182055at2759; -.
DR PhylomeDB; Q9WU63; -.
DR TreeFam; TF328887; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 56016; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9WU63; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9WU63; protein.
DR Bgee; ENSMUSG00000019853; Expressed in facial nucleus and 188 other tissues.
DR ExpressionAtlas; Q9WU63; baseline and differential.
DR Genevisible; Q9WU63; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:0035794; P:positive regulation of mitochondrial membrane permeability; ISO:MGI.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; ISO:MGI.
DR Gene3D; 3.20.80.10; -; 1.
DR InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR InterPro; IPR006917; SOUL_haem-bd.
DR PANTHER; PTHR11220; PTHR11220; 1.
DR Pfam; PF04832; SOUL; 1.
DR SUPFAM; SSF55136; SSF55136; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Mitochondrion; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Z4"
FT CHAIN 2..205
FT /note="Heme-binding protein 2"
FT /id="PRO_0000116901"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Z4"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Z4"
FT MUTAGEN 42
FT /note="H->A: Loss of heme binding."
FT /evidence="ECO:0000269|PubMed:15518569"
SQ SEQUENCE 205 AA; 23063 MW; 821B33F3E77DB05D CRC64;
MAEEPEPDLG VAEGSEDQAL EMPSWKAPED IDPQPGSYEI RHYGPAKWVS TCVESLDWDS
AIQTGFTKLN GYIQGKNEKE MKIKLTAPVT SYVEPGSSPF SESTITISLY IPSEQQPDPP
RPSESDVFIE DRAEMTVFVR SFDGFSSGQK NQEQLLTLAN ILREEGKVFN EKVFYTAGYS
SPFQLLDRNN EVWLIQKNEP SVENK
