ID   SR1B_PHYPO              Reviewed;         248 AA.
AC   P09351;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Spherulin-1B;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-209.
RX   PubMed=8587105; DOI=10.1007/bf00173188;
RA   Baumlein H., Braun H., Kakhovskaya I.A., Shutov A.D.;
RT   "Seed storage proteins of spermatophytes share a common ancestor with
RT   desiccation proteins of fungi.";
RL   J. Mol. Evol. 41:1070-1075(1995).
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall.
CC   -!- DEVELOPMENTAL STAGE: Accumulates specifically during spherulation.
CC   -!- MISCELLANEOUS: Spherulin is a major encystment-specific protein.
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; M18429; AAA29979.1; -; mRNA.
DR   EMBL; Z50151; CAA90512.1; -; Genomic_DNA.
DR   PIR; A29624; A29624.
DR   AlphaFoldDB; P09351; -.
DR   SMR; P09351; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR001929; Germin.
DR   InterPro; IPR019780; Germin_Mn-BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 1.
DR   PRINTS; PR00325; GERMIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00725; GERMIN; 1.
PE   2: Evidence at transcript level;
KW   Cell wall; Glycoprotein; Manganese; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..248
FT                   /note="Spherulin-1B"
FT                   /id="PRO_0000010847"
FT   DOMAIN          61..207
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         110
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   248 AA;  26435 MW;  0EFA506CC459ACEF CRC64;
     MQVRNILVAL VVVCFAVSEA ATQAPTSPPD SSASAEQVAQ LLNAPSELDR LKLLKDNQFV
     FDFKNSKLGV TQSAGGKTVA TSRTDFPAVI GHNIAMTVGF IEACGINLPH THPRATEINF
     IAKGRFQAGF FLENQATFIG HILEEGMATV FPQGAIHFEI NLECEPAMFV AAFNNEDPGV
     QTTASSFFGL PADVAAVSLN ISSIQTVEDL AKYLPHNPAI AMKECMQRCG MTGSSESSES
     SEDSSCSD