ID   PRF01_KALTU             Reviewed;         133 AA.
AC   C6JWH0;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Profilin Sal k 4.0101 {ECO:0000305};
DE   AltName: Full=Allergen Sal k 4 {ECO:0000303|PubMed:20622444};
DE   AltName: Allergen=Sal k 4.0101 {ECO:0000305};
OS   Kali turgidum (Prickly saltwort) (Salsola kali).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Salsoloideae; Salsoleae; Kali.
OX   NCBI_TaxID=151250 {ECO:0000312|EMBL:ACS34771.1};
RN   [1] {ECO:0000312|EMBL:ACS34771.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, AND
RP   ALLERGEN.
RC   TISSUE=Pollen {ECO:0000303|PubMed:20622444};
RX   PubMed=20622444; DOI=10.1271/bbb.100129;
RA   Assarehzadegan M.A., Amini A., Sankian M., Tehrani M., Jabbari F.,
RA   Varasteh A.;
RT   "Sal k 4, a new allergen of Salsola kali, is profilin: a predictive value
RT   of conserved conformational regions in cross-reactivity with other plant-
RT   derived profilins.";
RL   Biosci. Biotechnol. Biochem. 74:1441-1446(2010).
CC   -!- FUNCTION: Binds to actin and affects the structure of the cytoskeleton.
CC       At high concentrations, profilin prevents the polymerization of actin,
CC       whereas it enhances it at low concentrations.
CC       {ECO:0000255|RuleBase:RU003908}.
CC   -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC       actin in a 1:1 ratio. {ECO:0000255|RuleBase:RU003908}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P35081}.
CC   -!- TISSUE SPECIFICITY: Expressed in pollen. {ECO:0000269|PubMed:20622444}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 47% of
CC       the 30 patients allergic to S.kali pollen.
CC       {ECO:0000269|PubMed:20622444}.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000255,
CC       ECO:0000255|RuleBase:RU003909, ECO:0000305}.
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DR   EMBL; GQ145223; ACS34771.1; -; mRNA.
DR   AlphaFoldDB; C6JWH0; -.
DR   SMR; C6JWH0; -.
DR   Allergome; 2099; Sal k 4.
DR   Allergome; 8171; Sal k 4.0101.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   CDD; cd00148; PROF; 1.
DR   InterPro; IPR005455; PFN.
DR   InterPro; IPR036140; PFN_sf.
DR   InterPro; IPR027310; Profilin_CS.
DR   PANTHER; PTHR11604; PTHR11604; 1.
DR   Pfam; PF00235; Profilin; 1.
DR   PRINTS; PR00392; PROFILIN.
DR   PRINTS; PR01640; PROFILINPLNT.
DR   SMART; SM00392; PROF; 1.
DR   SUPFAM; SSF55770; SSF55770; 1.
DR   PROSITE; PS00414; PROFILIN; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Allergen; Cytoplasm; Cytoskeleton; Disulfide bond.
FT   CHAIN           1..133
FT                   /note="Profilin Sal k 4.0101"
FT                   /id="PRO_0000447665"
FT   DISULFID        95..117
FT                   /evidence="ECO:0000250|UniProtKB:Q8H2C9"
SQ   SEQUENCE   133 AA;  14272 MW;  2F9CAEA0F2513AD4 CRC64;
     MSWQTYVDDH LMCEIEGTNN HLTAAAILGV DGSVWAQSAN FPQFKPDEIS AVVKEFDEAG
     TLAPTGLHLG GTKYMVIQGE AGQVIRGKKG PGGICVKKTG QALIFGIYDE PVTPGQCNMI
     VERLGDYLVE QGM