CTHL2_SHEEP
ID CTHL2_SHEEP Reviewed; 176 AA.
AC P79362; P79363;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Cathelicidin-2;
DE AltName: Full=Bactenecin-5;
DE Short=Bac5;
DE AltName: Full=OaBac5;
DE Flags: Precursor;
GN Name=CATHL2; Synonyms=BAC5;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver;
RX PubMed=9461419; DOI=10.1016/s0378-1119(97)00569-6;
RA Huttner K.M., Lambeth M.R., Burkin H.R., Broad T.E.;
RT "Localization and genomic organization of sheep antimicrobial peptides
RT genes.";
RL Gene 206:85-91(1998).
CC -!- FUNCTION: Binds to the lipid A moiety of bacterial lipipolysaccharides
CC (LPS), a glycolipid present in the outer membrane of all Gram-negative
CC bacteria. Potent antimicrobial activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: BAC5 sequence consists almost exclusively of X-P-P-Y repeats.
CC -!- PTM: Elastase is responsible for its maturation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR EMBL; U60599; AAB49714.1; -; Genomic_DNA.
DR EMBL; U60601; AAB49716.1; -; mRNA.
DR RefSeq; NP_001009787.1; NM_001009787.1.
DR AlphaFoldDB; P79362; -.
DR SMR; P79362; -.
DR STRING; 9940.ENSOARP00000002071; -.
DR TCDB; 1.C.33.1.3; the cathelicidin (cathelicidin) family.
DR GeneID; 443356; -.
DR KEGG; oas:443356; -.
DR CTD; 100861213; -.
DR eggNOG; ENOG502SAES; Eukaryota.
DR OrthoDB; 1534863at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR001894; Cathelicidin-like.
DR InterPro; IPR018216; Cathelicidin_CS.
DR InterPro; IPR046350; Cystatin_sf.
DR PANTHER; PTHR10206; PTHR10206; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
DR PROSITE; PS00946; CATHELICIDINS_1; 1.
DR PROSITE; PS00947; CATHELICIDINS_2; 1.
PE 2: Evidence at transcript level;
KW Amidation; Antibiotic; Antimicrobial; Disulfide bond;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..130
FT /evidence="ECO:0000250"
FT /id="PRO_0000004706"
FT PEPTIDE 131..173
FT /note="Cathelicidin-2"
FT /id="PRO_0000004707"
FT PROPEP 174..176
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004708"
FT REGION 135..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P19660"
FT MOD_RES 173
FT /note="Proline amide"
FT /evidence="ECO:0000250"
FT DISULFID 85..96
FT /evidence="ECO:0000250"
FT DISULFID 107..124
FT /evidence="ECO:0000250"
FT CONFLICT 79
FT /note="T -> R (in Ref. 1; AAB49716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 19842 MW; 05080026EA6FD5F7 CRC64;
METQGASLSL GRWSLWLLLL GLVLPSASAQ ALSYREAVLR AVGQLNERSS EANLYRLLEL
DPAPNDEVDP GTRKPVSFTV KETVCPRTTQ QPPEECDFKE NGLVKQCVGT VTLDPSNDQF
DINCNELQSV RFRPPIRRPP IRPPFRPPFR PPVRPPIRPP FRPPFRPPIG PFPGRR
