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Stage IV sporulation protein A (EC 3.6.1.3) (Coat morphogenetic protein SpoIVA)

 SP4A_BACSU              Reviewed;         492 AA.
P35149;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
07-JUN-2017, entry version 105.
RecName: Full=Stage IV sporulation protein A;
EC=3.6.1.3;
AltName: Full=Coat morphogenetic protein SpoIVA;
Name=spoIVA; Synonyms=spoVP; OrderedLocusNames=BSU22800;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
DISRUPTION PHENOTYPE.
STRAIN=168 / PY79;
PubMed=1729246; DOI=10.1128/jb.174.2.575-585.1992;
Roels S., Driks A., Losick R.;
"Characterization of spoIVA, a sporulation gene involved in coat
morphogenesis in Bacillus subtilis.";
J. Bacteriol. 174:575-585(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
NCIMB 3610 / VKM B-501;
PubMed=1729247; DOI=10.1128/jb.174.2.586-594.1992;
Stevens C.M., Daniel R., Illing N., Errington J.;
"Characterization of a sporulation gene, spoIVA, involved in spore
coat morphogenesis in Bacillus subtilis.";
J. Bacteriol. 174:586-594(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
PROTEIN SEQUENCE OF 1-12, AND AMOUNT IN YABG MUTANT SPORES.
STRAIN=168;
PubMed=10714992; DOI=10.1128/JB.182.7.1883-1888.2000;
Takamatsu H., Kodama T., Imamura A., Asai K., Kobayashi K.,
Nakayama T., Ogasawara N., Watabe K.;
"The Bacillus subtilis yabG gene is transcribed by SigK RNA polymerase
during sporulation, and yabG mutant spores have altered coat protein
composition.";
J. Bacteriol. 182:1883-1888(2000).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=168 / PY79;
PubMed=8299942; DOI=10.1101/gad.8.2.234;
Driks A., Roels S., Beall B., Moran C.P. Jr., Losick R.;
"Subcellular localization of proteins involved in the assembly of the
spore coat of Bacillus subtilis.";
Genes Dev. 8:234-244(1994).
[6]
SUBCELLULAR LOCATION.
STRAIN=SG38;
PubMed=8936302; DOI=10.1099/00221287-142-4-733;
Lewis P.J., Errington J.;
"Use of green fluorescent protein for detection of cell-specific gene
expression and subcellular protein localization during sporulation in
Bacillus subtilis.";
Microbiology 142:733-740(1996).
[7]
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DOMAIN.
STRAIN=168 / PY79;
PubMed=9922240;
Price K.D., Losick R.;
"A four-dimensional view of assembly of a morphogenetic protein during
sporulation in Bacillus subtilis.";
J. Bacteriol. 181:781-790(1999).
[8]
CLEAVAGE BY YABG.
STRAIN=168;
PubMed=11040425; DOI=10.1111/j.1574-6968.2000.tb09355.x;
Takamatsu H., Imamura A., Kodama T., Asai K., Ogasawara N., Watabe K.;
"The yabG gene of Bacillus subtilis encodes a sporulation specific
protease which is involved in the processing of several spore coat
proteins.";
FEMS Microbiol. Lett. 192:33-38(2000).
[9]
MUTAGENESIS OF LEU-59; MET-69; CYS-98; ILE-210; ARG-230; VAL-241;
HIS-256; VAL-283; ILE-367; ILE-383; LEU-393; ILE-400; GLY-416;
GLU-418; VAL-453 AND ILE-457, AND DISRUPTION PHENOTYPE.
STRAIN=168 / PY79;
PubMed=11160095; DOI=10.1128/JB.183.5.1645-1654.2001;
Catalano F.A., Meador-Parton J., Popham D.L., Driks A.;
"Amino acids in the Bacillus subtilis morphogenetic protein SpoIVA
with roles in spore coat and cortex formation.";
J. Bacteriol. 183:1645-1654(2001).
[10]
FUNCTION, INTERACTION WITH SPOVM, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF GLY-486.
STRAIN=168 / PY79;
PubMed=17427285; DOI=10.1111/j.1365-2958.2006.05468.x;
Ramamurthi K.S., Clapham K.R., Losick R.;
"Peptide anchoring spore coat assembly to the outer forespore membrane
in Bacillus subtilis.";
Mol. Microbiol. 62:1547-1557(2006).
[11]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
SUBCELLULAR LOCATION, ATP-BINDING, MOTIF, DISRUPTION PHENOTYPE, AND
MUTAGENESIS OF LYS-30.
STRAIN=168 / PY79;
PubMed=18691972; DOI=10.1016/j.molcel.2008.05.030;
Ramamurthi K.S., Losick R.;
"ATP-driven self-assembly of a morphogenetic protein in Bacillus
subtilis.";
Mol. Cell 31:406-414(2008).
[12]
SUBUNIT, AND INTERACTION WITH SPOVID AND SAFA.
STRAIN=168 / PY79;
PubMed=19702880; DOI=10.1111/j.1574-6968.2009.01737.x;
Mullerova D., Krajcikova D., Barak I.;
"Interactions between Bacillus subtilis early spore coat morphogenetic
proteins.";
FEMS Microbiol. Lett. 299:74-85(2009).
[13]
INTERACTION WITH SPOVID, AND SUBCELLULAR LOCATION.
STRAIN=168 / PY79;
PubMed=19775244; DOI=10.1111/j.1365-2958.2009.06886.x;
Wang K.H., Isidro A.L., Domingues L., Eskandarian H.A., McKenney P.T.,
Drew K., Grabowski P., Chua M.H., Barry S.N., Guan M., Bonneau R.,
Henriques A.O., Eichenberger P.;
"The coat morphogenetic protein SpoVID is necessary for spore
encasement in Bacillus subtilis.";
Mol. Microbiol. 74:634-649(2009).
[14]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
SUBCELLULAR LOCATION, ATP-BINDING, AND MUTAGENESIS OF THR-70; THR-71;
ASP-97 AND SER-189.
STRAIN=168 / PY79;
PubMed=23267091; DOI=10.1073/pnas.1210554110;
Castaing J.P., Nagy A., Anantharaman V., Aravind L., Ramamurthi K.S.;
"ATP hydrolysis by a domain related to translation factor GTPases
drives polymerization of a static bacterial morphogenetic protein.";
Proc. Natl. Acad. Sci. U.S.A. 110:E151-E160(2013).
-!- FUNCTION: ATPase. Has a role at an early stage in the
morphogenesis of the spore coat outer layers. Its ATP hydrolysis
is required for proper assembly of the spore coat. Forms a
basement layer around the outside surface of the forespore and
self-assembles irreversibly into higher order structures by
binding and hydrolyzing ATP thus creating a durable and stable
platform upon which thereafter morphogenesis of the coat can take
place. Required for proper localization of spore coat protein CotE
and sporulation-specific proteins including SpoVM.
{ECO:0000269|PubMed:1729246, ECO:0000269|PubMed:17427285,
ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:23267091,
ECO:0000269|PubMed:8299942}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:23267091}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=412 uM for ATP {ECO:0000269|PubMed:18691972,
ECO:0000269|PubMed:23267091};
Note=The turnover rate is 2.7 pmol/min/pmol of SpoIVA at Vmax
(PubMed:18691972). The turnover rate is 1.0 pmol/min/pmol of
SpoIVA at Vmax (PubMed:23267091). {ECO:0000269|PubMed:18691972,
ECO:0000269|PubMed:23267091};
-!- SUBUNIT: Polymerizes to self-assemble into static filaments. ATP
hydrolysis is required by every subunit for incorporation into the
growing polymer by inducing a conformational change that drives
polymerization of a nucleotide-free filament. Polymerization
requires a critical concentration of the protein and only occurs
after it is localized to the surface of the developing spore.
Interacts (via extreme C-terminus Gly-486) with SpoVM (via Ile-6).
Interacts (via full-length) with SpoVID (via C-terminus 499-575
AA). Interacts with SafA. {ECO:0000269|PubMed:17427285,
ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:19702880,
ECO:0000269|PubMed:19775244, ECO:0000269|PubMed:23267091}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Uniformly
distributed on the membrane around the forespore, lying close to
or on its outer surface. Expression only necessary in the mother
cell chamber of the sporangium for the formation of a mature
spore. According to PubMed:8299942, not a coat protein of the
mature spore, is only transiently associated with the assembling
coat. According to PubMed:9922240, present as a component of the
fully mature spore. Proper localization requires the expression of
a gene spoVM which is under the control of the mother cell
transcription factor sigma E. {ECO:0000269|PubMed:1729247,
ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:18691972,
ECO:0000269|PubMed:19775244, ECO:0000269|PubMed:23267091,
ECO:0000269|PubMed:8299942, ECO:0000269|PubMed:8936302,
ECO:0000269|PubMed:9922240}.
-!- DEVELOPMENTAL STAGE: Expressed soon after the formation of the
asymmetric septum during sporulation. Expression commences about 2
hours after the onset of sporulation. Assembly around the
developing forespore commences at the time of polar division and
seems to continue after engulfment of the forespore is complete.
Remains present throughout the late stages of morphogenesis and
during this accumulation process preferentially collects on the
mother cell side of the engulfed forespore, but eventually is
deposited equally all around the forespore.
{ECO:0000269|PubMed:1729246, ECO:0000269|PubMed:1729247,
ECO:0000269|PubMed:9922240}.
-!- DOMAIN: Extreme C-terminal region (AA 487-492) is required for its
proper localization into a spherical shell around the developing
forespore. N-teminus (AA 1-64) is functionally important although
largely dispensable for proper localization.
{ECO:0000269|PubMed:9922240}.
-!- PTM: Seems to be cleaved by the YabG protease.
{ECO:0000269|PubMed:11040425}.
-!- DISRUPTION PHENOTYPE: Forespores lack a well-defined cortex, and
the coat is present as swirls in the mother cell compartment of
the sporangia rather than having been deposited around the
forespore protoplasts. According to PubMed:18691972, unable to
sporulate. {ECO:0000269|PubMed:11160095,
ECO:0000269|PubMed:1729246, ECO:0000269|PubMed:18691972}.
-!- MISCELLANEOUS: Present in an increased level in yabG mutant
spores.
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EMBL; M81169; AAA22802.1; -; Genomic_DNA.
EMBL; M80926; AAB59029.1; -; Genomic_DNA.
EMBL; AL009126; CAB14196.1; -; Genomic_DNA.
PIR; A41970; A41970.
RefSeq; NP_390161.1; NC_000964.3.
RefSeq; WP_003230572.1; NZ_JNCM01000036.1.
ProteinModelPortal; P35149; -.
STRING; 224308.Bsubs1_010100012526; -.
PaxDb; P35149; -.
EnsemblBacteria; CAB14196; CAB14196; BSU22800.
GeneID; 938991; -.
KEGG; bsu:BSU22800; -.
PATRIC; fig|224308.179.peg.2485; -.
eggNOG; ENOG4105DXU; Bacteria.
eggNOG; ENOG410XQ51; LUCA.
HOGENOM; HOG000058353; -.
KO; K06398; -.
OMA; RMVTTPW; -.
PhylomeDB; P35149; -.
BioCyc; BSUB:BSU22800-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0043595; C:endospore cortex; IMP:UniProtKB.
GO; GO:0042601; C:endospore-forming forespore; IDA:UniProtKB.
GO; GO:0031160; C:spore wall; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0000270; P:peptidoglycan metabolic process; IMP:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
GO; GO:0009847; P:spore germination; IMP:UniProtKB.
GO; GO:0042244; P:spore wall assembly; IDA:UniProtKB.
GO; GO:0070590; P:spore wall biogenesis; IDA:UniProtKB.
GO; GO:0043934; P:sporulation; IDA:UniProtKB.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IDA:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014201; Spore_IV_A.
Pfam; PF09547; Spore_IV_A; 1.
PIRSF; PIRSF007466; SpoIVA; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR02836; spore_IV_A; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Nucleotide-binding; Reference proteome; Sporulation.
CHAIN 1 492 Stage IV sporulation protein A.
/FTId=PRO_0000072073.
NP_BIND 24 31 ATP. {ECO:0000305}.
MOTIF 24 31 Walker A motif; involved in ATP-binding
and hydrolysis.
MUTAGEN 30 30 K->A: 20-fold reduction in sporulation
efficiency. Largely enriched at the
forespore periphery, although some
localization to the cytosol. Binding of
ATP reduced over 23-fold. Leads to
diminished ATP hydrolysis.
{ECO:0000269|PubMed:18691972}.
MUTAGEN 30 30 K->E: Mislocalized to the mother cell
cytosol. Misassembles the spore coat.
Mislocalizes CotE but not SpoVM. Does not
multimerize. Almost complete block in
spore formation.
{ECO:0000269|PubMed:18691972}.
MUTAGEN 59 59 L->P: Spores form largely normal coats
and possess at least some cortex, but
cannot remain dehydrated after mother
cell lysis. Abnormal synthesis and an
insufficient level of spore
peptidoglycan, which contains amidated
diaminopimelic acid, which is normally
found only in vegetative cell
peptidoglycan. Defective in germination;
when associated with P-256.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 69 69 M->L: Altered cortex and coat formation;
when associated with S-230.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 70 70 T->A: 500-fold decrease in sporulation
efficiency. 5-log decrease in sporulation
efficiency; no ATPase activity, but no
change in ATP-binding ability; unable to
polymerize and fails to promote coat
assembly; when associated with A-71.
{ECO:0000269|PubMed:23267091}.
MUTAGEN 71 71 T->A: Does not abrogate sporulation. 5-
log decrease in sporulation efficiency;
no ATPase activity, but no change in ATP-
binding ability; unable to polymerize and
fails to promote coat assembly; when
associated with A-70.
{ECO:0000269|PubMed:23267091}.
MUTAGEN 97 97 D->A: Completely abolished sporulation
efficiency. No ATPase activity, but no
change in ATP-binding ability. Unable to
polymerize and fails to promote coat
assembly;. {ECO:0000269|PubMed:23267091}.
MUTAGEN 98 98 C->S: Defective in germination; when
associated with N-283.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 189 189 S->K: Unable to sporulate.
{ECO:0000269|PubMed:23267091}.
MUTAGEN 210 210 I->A: Defective in germination; when
associated with V-367 and R-383.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 210 210 I->M: Altered cortex and coat formation;
when associated with V-367 and R-383.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 230 230 R->S: Altered cortex and coat formation;
when associated with L-69.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 241 241 V->G: Altered cortex and coat formation.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 256 256 H->P: Defective in germination; when
associated with P-59.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 283 283 V->N: Defective in germination; when
associated with S-98.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 367 367 I->V: Defective in germination; when
associated with A-210 and R-383. Altered
cortex and coat formation; when
associated with M-210 and R-383.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 383 383 I->R: Defective in germination; when
associated with A-210 and V-367. Altered
cortex and coat formation; when
associated with M-210 and R-383.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 393 393 L->P: Altered cortex and coat formation.
Possesses swirls of coat in the mother
cell cytoplasm and does not possess a
cortex. {ECO:0000269|PubMed:11160095}.
MUTAGEN 400 400 I->P: Altered cortex and coat formation,
affects localization to the forespore;
when associated with R-457 and V-418.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 416 416 G->R: Altered cortex and coat formation.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 418 418 E->V: Altered cortex and coat formation,
affects localization to the forespore;
when associated with P-400 and R-457.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 453 453 V->G: Altered cortex and coat formation,
affects localization to the forespore.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 457 457 I->R: Altered cortex and coat formation,
affects localization to the forespore;
when associated with P-400 and V-418.
{ECO:0000269|PubMed:11160095}.
MUTAGEN 486 486 G->V: Suppressor mutation that reverses
the mislocalization and sporulation
defect of the A-6 mutation in SpoVM.
Causes little impairment of sporulation.
{ECO:0000269|PubMed:17427285}.
SEQUENCE 492 AA; 55175 MW; 29EBA349DD18D12A CRC64;
MEKVDIFKDI AERTGGDIYL GVVGAVRTGK STFIKKFMEL VVLPNISNEA DRARAQDELP
QSAAGKTIMT TEPKFVPNQA MSVHVSDGLD VNIRLVDCVG YTVPGAKGYE DENGPRMINT
PWYEEPIPFH EAAEIGTRKV IQEHSTIGVV ITTDGTIGDI ARSDYIEAEE RVIEELKEVG
KPFIMVINSV RPYHPETEAM RQDLSEKYDI PVLAMSVESM RESDVLSVLR EALYEFPVLE
VNVNLPSWVM VLKENHWLRE SYQESVKETV KDIKRLRDVD RVVGQFSEFE FIESAGLAGI
ELGQGVAEID LYAPDHLYDQ ILKEVVGVEI RGRDHLLELM QDFAHAKTEY DQVSDALKMV
KQTGYGIAAP ALADMSLDEP EIIRQGSRFG VRLKAVAPSI HMIKVDVESE FAPIIGTEKQ
SEELVRYLMQ DFEDDPLSIW NSDIFGRSLS SIVREGIQAK LSLMPENARY KLKETLERII
NEGSGGLIAI IL


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orb71713 Influenza A M2 coat protein (22-46) peptide This is Influenza A M2 coat protein (22-46) peptide. For research use only. 1 mg
U0014h CLIA BMP2B,BMP-2B,BMP4,BMP-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,DVR4,Homo sapiens,Human 96T
E0014h ELISA BMP2B,BMP-2B,BMP4,BMP-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,DVR4,Homo sapiens,Human 96T
E0014h ELISA kit BMP2B,BMP-2B,BMP4,BMP-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,DVR4,Homo sapiens,Human 96T
E0013h ELISA BMP2,BMP-2,BMP2A,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Homo sapiens,Human 96T
U0013h CLIA BMP2,BMP-2,BMP2A,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Homo sapiens,Human 96T


 

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