LATH_HORSE
ID LATH_HORSE Reviewed; 228 AA.
AC P82615; P82616; Q8SPI9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Latherin;
DE AltName: Full=Dander allergen Equ c 4/Equ c 5;
DE AltName: Allergen=Equ c 4;
DE Flags: Precursor;
GN Name=LATH;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Sweat gland;
RA Fleming R.I., Beeley J.G., Cooper A., Jones J.T., Matthews J.B.,
RA Kennedy M.W.;
RT "Latherin -- the surfactant protein and allergen of horse sweat.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 76-129 AND 148-158, GLYCOSYLATION, AND ALLERGEN.
RC TISSUE=Dander;
RX PubMed=11358533; DOI=10.1046/j.1432-1327.2001.02217.x;
RA Goubran Botros H., Poncet P., Rabillon J., Fontaine T., Laval J.-M.,
RA David B.;
RT "Biochemical characterization and surfactant properties of horse
RT allergens.";
RL Eur. J. Biochem. 268:3126-3136(2001).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=3753435; DOI=10.1042/bj2350645;
RA Beeley J.G., Eason R., Snow D.H.;
RT "Isolation and characterization of latherin, a surface-active protein from
RT horse sweat.";
RL Biochem. J. 235:645-650(1986).
RN [4]
RP STRUCTURE BY NMR OF 20-228, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=23782536; DOI=10.1098/rsif.2013.0453;
RA Vance S.J., McDonald R.E., Cooper A., Smith B.O., Kennedy M.W.;
RT "The structure of latherin, a surfactant allergen protein from horse sweat
RT and saliva.";
RL J. R. Soc. Interface 10:20130453-20130453(2013).
CC -!- FUNCTION: Major protein in sweat, has surfactant properties. Has a role
CC in temperature regulation by having a capacity to make hydrophobic
CC surfaces wettable and so can function in promoting spreading and
CC evaporation of sweat. {ECO:0000269|PubMed:3753435}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23782536}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Found in sweat (at protein level).
CC {ECO:0000269|PubMed:3753435}.
CC -!- PTM: No sign of N-X-[ST] acceptor site even though reported as N-
CC glycosylated. {ECO:0000269|PubMed:11358533}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Allergen of horse
CC dander. {ECO:0000269|PubMed:11358533}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. Plunc family.
CC {ECO:0000305}.
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DR EMBL; AF491288; AAM09530.3; -; mRNA.
DR RefSeq; NP_001075328.2; NM_001081859.2.
DR PDB; 3ZPM; NMR; -; A=21-228.
DR PDBsum; 3ZPM; -.
DR AlphaFoldDB; P82615; -.
DR BMRB; P82615; -.
DR SMR; P82615; -.
DR Allergome; 3303; Equ c 4.0101.
DR Allergome; 336; Equ c 4.
DR PaxDb; P82615; -.
DR PeptideAtlas; P82615; -.
DR GeneID; 100033921; -.
DR KEGG; ecb:100033921; -.
DR CTD; 100033921; -.
DR InParanoid; P82615; -.
DR OrthoDB; 1051740at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0050828; P:regulation of liquid surface tension; IDA:CACAO.
DR GO; GO:0001659; P:temperature homeostasis; IDA:CACAO.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR032953; Latherin.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR47015:SF3; PTHR47015:SF3; 1.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR SUPFAM; SSF55394; SSF55394; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..228
FT /note="Latherin"
FT /id="PRO_0000017190"
FT DISULFID 153..196
FT /evidence="ECO:0000269|PubMed:23782536"
FT CONFLICT 88
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 25..41
FT /evidence="ECO:0007829|PDB:3ZPM"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:3ZPM"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:3ZPM"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:3ZPM"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3ZPM"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3ZPM"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3ZPM"
FT STRAND 99..121
FT /evidence="ECO:0007829|PDB:3ZPM"
FT STRAND 124..140
FT /evidence="ECO:0007829|PDB:3ZPM"
FT STRAND 146..164
FT /evidence="ECO:0007829|PDB:3ZPM"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3ZPM"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:3ZPM"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:3ZPM"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:3ZPM"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:3ZPM"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3ZPM"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:3ZPM"
SQ SEQUENCE 228 AA; 24701 MW; 544088871FBEFF92 CRC64;
MLKVSCLFVL LCGLLVPSSA QQIPPEVSSQ ITDALTQGLL DGNFLSLLNA INLEGLLNTI
LDQVTGLLNI LVGPLLGPSD AEIKLQDTRL LQLSLEFSPD SKGIDIWIPL ELSVYLKLLI
LEPLTLYVRT DIRVQLRLES DEDGKYRLAF GHCSLLPRAI ELQSGNPLSL PVNAVLGTIE
NALGNFITED LGAGLCPTLN SLVSNLDLQL VNNLINLILD RANVDLSV
