SR3A_PHYPO
ID SR3A_PHYPO Reviewed; 103 AA.
AC P09353;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Spherulin-3A;
DE Short=S3A;
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2830170; DOI=10.1016/0378-1119(87)90334-9;
RA Bernier F., Lemieux G., Pallotta D.;
RT "Gene families encode the major encystment-specific proteins of Physarum
RT polycephalum plasmodia.";
RL Gene 59:265-277(1987).
RN [2]
RP SIMILARITY TO BETA/GAMMA CRYSTALLINS.
RX PubMed=2107329; DOI=10.1007/bf02099940;
RA Wistow G.;
RT "Evolution of a protein superfamily: relationships between vertebrate lens
RT crystallins and microorganism dormancy proteins.";
RL J. Mol. Evol. 30:140-145(1990).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=9281431; DOI=10.1006/jmbi.1997.1184;
RA Rosinke B., Renner C., Mayr E.-M., Jaenicke R., Holak T.A.;
RT "Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype
RT gamma-crystallin fold in aqueous solution.";
RL J. Mol. Biol. 271:645-655(1997).
CC -!- FUNCTION: Structural protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Major encystment-specific protein.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; M18431; AAA29981.1; -; mRNA.
DR PIR; D29624; D29624.
DR PDB; 1AG4; NMR; -; A=1-103.
DR PDB; 1HDF; X-ray; 2.35 A; A/B=2-103.
DR PDBsum; 1AG4; -.
DR PDBsum; 1HDF; -.
DR AlphaFoldDB; P09353; -.
DR SMR; P09353; -.
DR EvolutionaryTrace; P09353; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR015059; Ca_cell_adhesion_N_dom.
DR InterPro; IPR011024; G_crystallin-like.
DR Pfam; PF08964; Crystall_3; 1.
DR SMART; SM00247; XTALbg; 1.
DR SUPFAM; SSF49695; SSF49695; 1.
DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Repeat.
FT CHAIN 1..103
FT /note="Spherulin-3A"
FT /id="PRO_0000057608"
FT DOMAIN 14..55
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 57..99
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 1..13
FT /note="N-terminal arm"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1HDF"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1HDF"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1HDF"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:1HDF"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1HDF"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1HDF"
FT TURN 42..47
FT /evidence="ECO:0007829|PDB:1HDF"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1HDF"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1HDF"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1HDF"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1HDF"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1HDF"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1HDF"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1AG4"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1HDF"
SQ SEQUENCE 103 AA; 11285 MW; 4D92B1988B965E6D CRC64;
MSVCKGVSGN PAKGEVFLYK HVNFQGDSWK VTGNVYDFRS VSGLNDVVSS VKVGPNTKAF
IFKDDRFNGN FIRLEESSQV TDLTTRNLND AISSIIVATF ESA
