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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}.
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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
 
 
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