LI601_CANLF
ID LI601_CANLF Reviewed; 190 AA.
AC H2B3G5;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Lipocalin Can f 6.0101 {ECO:0000303|PubMed:22104604};
DE AltName: Full=Allergen Can f 6 {ECO:0000303|PubMed:22515174, ECO:0000303|PubMed:29207604, ECO:0000303|PubMed:30728436};
DE AltName: Allergen=Can f 6.0101 {ECO:0000303|PubMed:22104604};
DE Flags: Precursor;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000312|EMBL:CCF72371.1};
RN [1] {ECO:0000312|EMBL:CCF72371.1}
RP NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, AND
RP ALLERGEN.
RC TISSUE=Submandibular gland {ECO:0000303|PubMed:22104604};
RX PubMed=22104604; DOI=10.1016/j.jaci.2011.10.017;
RA Hilger C., Swiontek K., Arumugam K., Lehners C., Hentges F.;
RT "Identification of a new major dog allergen highly cross-reactive with Fel
RT d 4 in a population of cat- and dog-sensitized patients.";
RL J. Allergy Clin. Immunol. 129:1149-1151(2012).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer {ECO:0000303|PubMed:16341006};
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [3]
RP SUBUNIT, TISSUE SPECIFICITY, ALLERGEN, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=22515174; DOI=10.1111/j.1398-9995.2012.02826.x;
RA Nilsson O.B., Binnmyr J., Zoltowska A., Saarne T., van Hage M.,
RA Groenlund H.;
RT "Characterization of the dog lipocalin allergen Can f 6: the role in cross-
RT reactivity with cat and horse.";
RL Allergy 67:751-757(2012).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND ALLERGEN.
RX PubMed=23464525; DOI=10.1111/all.12130;
RA Polovic N., Waden K., Binnmyr J., Hamsten C., Groenneberg R., Palmberg C.,
RA Milcic-Matic N., Bergman T., Groenlund H., van Hage M.;
RT "Dog saliva - an important source of dog allergens.";
RL Allergy 68:585-592(2013).
RN [5]
RP ALLERGEN.
RX PubMed=23464491; DOI=10.1111/all.12107;
RA Jakob T., Hilger C., Hentges F.;
RT "Clinical relevance of sensitization to cross-reactive lipocalin Can f 6.";
RL Allergy 68:690-691(2013).
RN [6]
RP 3D-STRUCTURE MODELING, ALLERGEN, REGION, AND SYNTHESIS OF 43-54; 76-83;
RP 91-97; 100-109; 125-132 AND 139-152.
RX PubMed=29207604; DOI=10.18632/oncotarget.21822;
RA Wang Y.J., Li L., Song W.J., Zhou Y.J., Cao M.D., Zuo X.R., Wei J.F.;
RT "Canis familiaris allergen Can f 6: expression, purification and analysis
RT of B-cell epitopes in Chinese dog allergic children.";
RL Oncotarget 8:90796-90807(2017).
RN [7] {ECO:0007744|PDB:5X7Y}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 16-190, SUBUNIT, ALLERGEN,
RP DISULFIDE BOND, MUTAGENESIS OF 30-SER--ILE-32; 46-LYS--LYS-48;
RP 50-GLU--ASN-52; 115-TYR--ASP-117 AND 128-GLN--GLN-130, AND CIRCULAR
RP DICHROISM ANALYSIS.
RX PubMed=30728436; DOI=10.1038/s41598-018-38134-w;
RA Yamamoto K., Ishibashi O., Sugiura K., Ubatani M., Sakaguchi M.,
RA Nakatsuji M., Shimamoto S., Noda M., Uchiyama S., Fukutomi Y.,
RA Nishimura S., Inui T.;
RT "Crystal structure of the dog allergen Can f 6 and structure-based
RT implications of its cross-reactivity with the cat allergen Fel d 4.";
RL Sci. Rep. 9:1503-1503(2019).
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22515174,
CC ECO:0000269|PubMed:30728436}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23464525,
CC ECO:0000305|PubMed:22515174}.
CC -!- TISSUE SPECIFICITY: Expressed in saliva (at protein level)
CC (PubMed:23464525). Expressed in dander (at protein level)
CC (PubMed:22515174, PubMed:23464525). According to PubMed:22104604,
CC expressed in submaxillary gland (PubMed:22104604). In contrast,
CC according to PubMed:22515174, not expressed in submaxillary gland.
CC Expressed in bladder and skin, but not in tongue (PubMed:22515174).
CC {ECO:0000269|PubMed:22104604, ECO:0000269|PubMed:22515174,
CC ECO:0000269|PubMed:23464525}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE
CC (PubMed:22104604, PubMed:22515174, PubMed:23464525, PubMed:23464491,
CC PubMed:29207604, PubMed:30728436). Binds to IgE in 61% of the 44
CC patients tested allergic to both dog and cat dander (PubMed:22104604).
CC Binds to IgE in 38% of the 100 patients tested allergic to dog dander
CC (PubMed:22515174). Binds to IgE in all 3 patients tested allergic to
CC both dog and horse dander (PubMed:23464491). Binds to IgE in 56% of the
CC 32 Chinese children tested allergic to dog (PubMed:29207604). Binds to
CC IgE in 47% of the 38 patients tested allergic to dog dander
CC (PubMed:30728436). Causes activation of human basophils
CC (PubMed:22515174, PubMed:29207604). {ECO:0000269|PubMed:22104604,
CC ECO:0000269|PubMed:22515174, ECO:0000269|PubMed:23464491,
CC ECO:0000269|PubMed:23464525, ECO:0000269|PubMed:29207604,
CC ECO:0000269|PubMed:30728436}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000255, ECO:0000255|RuleBase:RU003695, ECO:0000305}.
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DR EMBL; HE653774; CCF72371.1; -; mRNA.
DR EMBL; AAEX03008079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001271390.1; NM_001284461.1.
DR RefSeq; XP_855342.1; XM_850249.3.
DR PDB; 5X7Y; X-ray; 2.35 A; A/B/C/D=16-190.
DR PDB; 6NRE; X-ray; 2.06 A; A=16-190.
DR PDBsum; 5X7Y; -.
DR PDBsum; 6NRE; -.
DR AlphaFoldDB; H2B3G5; -.
DR SMR; H2B3G5; -.
DR STRING; 9615.ENSCAFP00000057458; -.
DR Allergome; 9406; Can f 6.
DR Ensembl; ENSCAFT00030045368; ENSCAFP00030039616; ENSCAFG00030024661.
DR Ensembl; ENSCAFT00040029774; ENSCAFP00040025863; ENSCAFG00040016155.
DR Ensembl; ENSCAFT00845012656; ENSCAFP00845009874; ENSCAFG00845007127.
DR GeneID; 481674; -.
DR KEGG; cfa:481674; -.
DR VEuPathDB; HostDB:ENSCAFG00845007127; -.
DR GeneTree; ENSGT01050000244868; -.
DR OrthoDB; 1475169at2759; -.
DR Proteomes; UP000002254; Chromosome 11.
DR Bgee; ENSCAFG00000003064; Expressed in saliva-secreting gland and 46 other tissues.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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; IPR002971; Maj_urinary.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01221; MAJORURINARY.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..190
FT /note="Lipocalin Can f 6.0101"
FT /evidence="ECO:0000255"
FT /id="PRO_5012858929"
FT REGION 43..54
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:29207604"
FT REGION 76..83
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:29207604"
FT REGION 91..97
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:29207604"
FT REGION 100..109
FT /note="No IgE-binding"
FT /evidence="ECO:0000269|PubMed:29207604"
FT REGION 125..132
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:29207604"
FT REGION 139..152
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:29207604"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 82..175
FT /evidence="ECO:0000269|PubMed:30728436,
FT ECO:0007744|PDB:5X7Y"
FT MUTAGEN 30..32
FT /note="SKI->AAA: Decreased IgE reactivity by approximately
FT 7% compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30728436"
FT MUTAGEN 46..48
FT /note="KEK->AAA: Decreased IgE reactivity by approximately
FT 15% compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30728436"
FT MUTAGEN 50..52
FT /note="EEN->AAA: Decreased IgE reactivity by approximately
FT 15% compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30728436"
FT MUTAGEN 115..117
FT /note="YED->AAA: No effect on IgE reactivity."
FT /evidence="ECO:0000269|PubMed:30728436"
FT MUTAGEN 128..130
FT /note="QEQ->AAA: No effect on IgE reactivity."
FT /evidence="ECO:0000269|PubMed:30728436"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:6NRE"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:6NRE"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6NRE"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:6NRE"
FT STRAND 66..78
FT /evidence="ECO:0007829|PDB:6NRE"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:6NRE"
FT STRAND 97..114
FT /evidence="ECO:0007829|PDB:6NRE"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6NRE"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:6NRE"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:6NRE"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:6NRE"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6NRE"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6NRE"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6NRE"
SQ SEQUENCE 190 AA; 21825 MW; 5A0CB28EC4F055C7 CRC64;
MKLLLLCLGL ILVHAHEEEN DVVKGNFDIS KISGDWYSIL LASDIKEKIE ENGSMRVFVK
DIEVLSNSSL IFTMHTKVNG KCTKISLICN KTEKDGEYDV VHDGYNLFRI IETAYEDYII
FHLNNVNQEQ EFQLMELYGR KPDVSPKVKE KFVRYCQGME IPKENILDLT QVDRCLQARQ
SEAAQVSSAE
