AVP2_CAVPO
ID AVP2_CAVPO Reviewed; 170 AA.
AC P83508; F0UZ11;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Lipocalin Cav p 2.0101 {ECO:0000303|PubMed:21518038};
DE AltName: Full=Major allergen Cav p 2 {ECO:0000303|PubMed:12823123};
DE AltName: Allergen=Cav p 2.0101 {ECO:0000303|PubMed:21518038};
DE Flags: Precursor;
GN Name=Lcncavp2 {ECO:0000312|Ensembl:ENSCPOP00000025189};
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:0000305};
RN [1] {ECO:0000312|EMBL:CAX62129.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-31, TISSUE SPECIFICITY,
RP PTM, AND ALLERGEN.
RC STRAIN=Dunkin-Hartley {ECO:0000303|PubMed:21518038,
RC ECO:0000312|EMBL:CAX62129.1};
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:ENSCPOP00000025189, ECO:0000312|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000312|Ensembl:ENSCPOP00000025189,
RC ECO:0000312|Proteomes:UP000005447};
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).
RN [3]
RP PROTEIN SEQUENCE OF 17-31, TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Hair {ECO:0000303|PubMed:12823123};
RX PubMed=12823123; DOI=10.1034/j.1398-9995.2003.00177.x;
RA Fahlbusch B., Rudeschko O., Schlott B., Henzgen M., Schlenvoigt G.,
RA Schubert H., Kinne R.W.;
RT "Further characterization of IgE-binding antigens from guinea pig hair as
RT new members of the lipocalin family.";
RL Allergy 58:629-634(2003).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12823123,
CC ECO:0000305|PubMed:21518038}.
CC -!- TISSUE SPECIFICITY: Expressed in harderian gland (at protein level)
CC (PubMed:21518038). Expressed in hair (at protein level)
CC (PubMed:21518038, PubMed:12823123). Expressed in submaxillary gland and
CC harderian gland (PubMed:21518038). {ECO:0000269|PubMed:12823123,
CC ECO:0000269|PubMed:21518038}.
CC -!- PTM: Not N-linked glycosylated. {ECO:0000269|PubMed:21518038}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE
CC (PubMed:21518038, PubMed:12823123). Binds to IgE in 65% of the 26
CC patients tested allergic to guinea pigs (PubMed:21518038). Is a cause
CC of guinea pig hair allergy (PubMed:12823123). Causes degranulation of
CC humanized rat basophil leukemia cells (RBL) and release of beta-
CC hexosaminidase (PubMed:21518038). {ECO:0000269|PubMed:12823123,
CC ECO:0000269|PubMed:21518038}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; FN256284; CAX62129.1; -; mRNA.
DR EMBL; AAKN02052698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001192113.1; NM_001205184.1.
DR AlphaFoldDB; P83508; -.
DR SMR; P83508; -.
DR Allergome; 3183; Cav p 2.0101.
DR Allergome; 618; Cav p 2.
DR Ensembl; ENSCPOT00000035307; ENSCPOP00000025189; ENSCPOG00000037628.
DR GeneID; 100534654; -.
DR KEGG; cpoc:100534654; -.
DR CTD; 100534654; -.
DR GeneTree; ENSGT01050000244868; -.
DR OrthoDB; 1357921at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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; 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.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:12823123,
FT ECO:0000269|PubMed:21518038"
FT CHAIN 17..170
FT /note="Lipocalin Cav p 2.0101"
FT /evidence="ECO:0000305|PubMed:12823123,
FT ECO:0000305|PubMed:21518038"
FT /id="PRO_0000201031"
FT DISULFID 56..60
FT /evidence="ECO:0000250|UniProtKB:P08937"
FT DISULFID 75..168
FT /evidence="ECO:0000250|UniProtKB:P08937"
SQ SEQUENCE 170 AA; 18736 MW; 3AB8DCCBA7C4322A CRC64;
MMQILLLALA VSLACADSID YSKVPGNWRT IAIAADHVEK IEVNGELRAY FRQVDCTEGC
DKISITFYTN TDGVCTEHTV VGARNGENDV YTVDYAGENT FQILCNSDDA FVIGSVNTDQ
NGQTTKEVAI AAKRNFLTPE QEQKFQKAVQ NAGIPLENIR YVIETDTCPD
