SR1A_PHYPO
ID SR1A_PHYPO Reviewed; 246 AA.
AC P09350;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Spherulin-1A;
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 PROTEIN SEQUENCE OF 20-34.
RX PubMed=1425703; DOI=10.1111/j.1432-1033.1992.tb17369.x;
RA Lane B.G., Cuming A.C., Fregeau J., Carpita N.C., Hurkman W.J., Bernier F.,
RA Dratewka-Kos E., Kennedy T.D.;
RT "Germin isoforms are discrete temporal markers of wheat development.
RT Pseudogermin is a uniquely thermostable water-soluble oligomeric protein in
RT ungerminated embryos and like germin in germinated embryos, it is
RT incorporated into cell walls.";
RL Eur. J. Biochem. 209:961-969(1992).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M18428; AAA29982.1; -; mRNA.
DR PIR; B29624; B29624.
DR AlphaFoldDB; P09350; -.
DR SMR; P09350; -.
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 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Glycoprotein; Manganese;
KW Metal-binding; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1425703"
FT CHAIN 20..246
FT /note="Spherulin-1A"
FT /id="PRO_0000010846"
FT DOMAIN 74..220
FT /note="Cupin type-1"
FT /evidence="ECO:0000255"
FT REGION 23..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 246 AA; 26138 MW; A06360A64A1B8BD2 CRC64;
MKSTFLFALF VLFLAASEAA TDYPTNPPTT PPTPAPTSTP LPSSAASPEL VAQLLNAPSE
LDRIKLLKDN QFVFDFKNSK LGVTQGTGGK TVATSRTNFP AVIGHNVAMT VGFIEACGIN
LPHTHPRATE INFIASGKFE AGFFLENQAK FIGHTLEAGM ATVFPQGAIH FEINMNCEPA
MFVAAFNNED PGVQTTASSF FGLPADVVGV SLNISSIQTV EDLGKHLPQN PAVAMQACMK
RCGFSD