ID   FABH_ASCSU              Reviewed;         163 AA.
AC   P55776;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Fatty acid-binding protein homolog;
DE   AltName: Full=AS-P18;
DE   Flags: Precursor;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING.
RX   PubMed=9092532; DOI=10.1074/jbc.272.15.9933;
RA   Mei B., Kennedy M.W., Beauchamp J., Komuniecki P.R., Komuniecki R.;
RT   "Secretion of a novel, developmentally regulated fatty acid-binding protein
RT   into the perivitelline fluid of the parasitic nematode, Ascaris suum.";
RL   J. Biol. Chem. 272:9933-9941(1997).
CC   -!- FUNCTION: May play a role in sequestering potentially toxic fatty acids
CC       and their peroxidation products, or it may be involved in the
CC       maintenance of the impermeable lipid layer of the eggshell.
CC   -!- TISSUE SPECIFICITY: Abundant in the fluid surrounding the developing
CC       embryo of Ascaris suum.
CC   -!- DEVELOPMENTAL STAGE: Synthesis appears to be switched off shortly after
CC       hatching from the egg and invasion of the host. P18 is not found in
CC       unembryonated eggs, begins to be synthesized at about day 3 of
CC       development, reaches a maximal concentration with the formation of the
CC       first-stage larva and remains abundant in the perivitelline fluid of
CC       the second-stage larva.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   EMBL; U51906; AAA98565.1; -; mRNA.
DR   PDB; 6I8X; X-ray; 2.30 A; A/B=21-163.
DR   PDB; 6I9F; NMR; -; A=21-163.
DR   PDBsum; 6I8X; -.
DR   PDBsum; 6I9F; -.
DR   AlphaFoldDB; P55776; -.
DR   BMRB; P55776; -.
DR   SMR; P55776; -.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR040094; Lbp1-4.
DR   PANTHER; PTHR22725; PTHR22725; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lipid-binding; Signal; Transport.
FT   SIGNAL          1..23
FT   CHAIN           24..163
FT                   /note="Fatty acid-binding protein homolog"
FT                   /id="PRO_0000008736"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          29..38
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   HELIX           39..45
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   HELIX           50..57
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          76..84
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          105..116
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          119..128
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          133..141
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          144..151
FT                   /evidence="ECO:0007829|PDB:6I8X"
FT   STRAND          154..162
FT                   /evidence="ECO:0007829|PDB:6I8X"
SQ   SEQUENCE   163 AA;  19077 MW;  98F06D019A73E3C3 CRC64;
     MRCLVALILT VLIVTPEVEA KTLPDKFLGT FKLERDENFD EYLKARGYGW IMRQVIKLAG
     VTKKFRNAAS GKPDRYDMEN LTTKKDTHHK DWALGEEFQD EALDSTQHKI TFDLKDPNTL
     TETHIKVDDP TDVETYEYRR DGDYLVMKMS WKGVSTSRYY KKQ