ID   AVP3_CAVPO              Reviewed;         170 AA.
AC   F0UZ12; H0W0A8;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Lipocalin Cav p 3.0101 {ECO:0000303|PubMed:21518038, ECO:0000312|EMBL:CAX62130.1};
DE   AltName: Allergen=Cav p 3.0101 {ECO:0000303|PubMed:21518038};
DE   Flags: Precursor;
GN   Name=Lcncavp3 {ECO:0000312|Ensembl:ENSCPOP00000016393};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000312|EMBL:CAX62130.1};
RN   [1] {ECO:0000312|EMBL:CAX62130.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-30, TISSUE SPECIFICITY,
RP   PTM, AND ALLERGEN.
RC   STRAIN=Dunkin-Hartley {ECO:0000303|PubMed:21518038,
RC   ECO:0000312|EMBL:CAX62130.1};
RC   TISSUE=Submandibular gland {ECO:0000303|PubMed:21518038};
RX   PubMed=21518038; DOI=10.1111/j.1365-2222.2011.03726.x;
RA   Hilger C., Swiontek K., Kler S., Diederich C., Lehners C., Vogel L.,
RA   Vieths S., Hentges F.;
RT   "Evaluation of two new recombinant guinea-pig lipocalins, Cav p 2 and Cav p
RT   3, in the diagnosis of guinea-pig allergy.";
RL   Clin. Exp. Allergy 41:899-908(2011).
RN   [2] {ECO:0000312|Ensembl:ENSCPOP00000016393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000312|Ensembl:ENSCPOP00000016393};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21518038}.
CC   -!- TISSUE SPECIFICITY: Expressed in submaxillary gland (at protein level).
CC       {ECO:0000303|PubMed:21518038}.
CC   -!- PTM: Not N-linked glycosylated. {ECO:0000269|PubMed:21518038}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 54% of
CC       the 26 patients tested allergic to guinea pigs. Causes degranulation of
CC       humanized rat basophil leukemia cells (RBL) and release of beta-
CC       hexosaminidase. {ECO:0000269|PubMed:21518038}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000255, ECO:0000255|RuleBase:RU003695, ECO:0000305}.
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DR   EMBL; FN256285; CAX62130.1; -; mRNA.
DR   EMBL; AAKN02052703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001192114.1; NM_001205185.1.
DR   AlphaFoldDB; F0UZ12; -.
DR   SMR; F0UZ12; -.
DR   Allergome; 8178; Cav p 3.
DR   Allergome; 8181; Cav p 3.0101.
DR   Ensembl; ENSCPOT00000022469; ENSCPOP00000016393; ENSCPOG00000020220.
DR   GeneID; 100534655; -.
DR   KEGG; cpoc:100534655; -.
DR   CTD; 100534655; -.
DR   eggNOG; ENOG502TDZD; Eukaryota.
DR   GeneTree; ENSGT01050000244868; -.
DR   HOGENOM; CLU_094061_4_2_1; -.
DR   OMA; WHTISIA; -.
DR   OrthoDB; 1357921at2759; -.
DR   TreeFam; TF338197; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000020220; Expressed in cerebellum.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR002345; Lipocalin.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   InterPro; IPR002448; OBP-like.
DR   PANTHER; PTHR11430; PTHR11430; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR01173; ODORANTBNDNG.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:21518038"
FT   CHAIN           16..170
FT                   /note="Lipocalin Cav p 3.0101"
FT                   /evidence="ECO:0000305|PubMed:21518038"
FT                   /id="PRO_5014089049"
FT   DISULFID        56..60
FT                   /evidence="ECO:0000250|UniProtKB:P08937"
FT   DISULFID        75..168
FT                   /evidence="ECO:0000250|UniProtKB:P08937"
FT   CONFLICT        16
FT                   /note="H -> G (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   170 AA;  19157 MW;  0B4D70D118931AF4 CRC64;
     MQILLLALTI GLAYAHQTLD PSEINGQWHT ISIAADNVEK IGEGGPLRGY FHNLHCYDGC
     KNIGLTFYVK LDGNCQRFDV LGAKQEDSDV YVAQYSGTNH FEVIGKKEDA IAFYNHNTDE
     TGKETKMIVV VARRDSLTEE EQQKLQEVAG EKGIPKDNIR YFRERDTCAQ