ID   SC51_SHEEP              Reviewed;         160 AA.
AC   P49928;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Cathelin-related peptide SC5;
DE   AltName: Full=Antibacterial peptide SMAP-29;
DE   AltName: Full=Myeloid antibacterial peptide MAP-29;
DE   Flags: Precursor;
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 [MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=8549789; DOI=10.1016/0014-5793(95)01390-3;
RA   Mahoney M.M., Lee A.Y., Brezinski-Caliguri D.J., Huttner K.M.;
RT   "Molecular analysis of the sheep cathelin family reveals a novel
RT   antimicrobial peptide.";
RL   FEBS Lett. 377:519-522(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN   [3]
RP   STRUCTURE BY NMR OF 132-160.
RX   PubMed=11856344; DOI=10.1046/j.0014-2956.2002.02751.x;
RA   Tack B.F., Sawai M.V., Kearney W.R., Robertson A.D., Sherman M.A., Wang W.,
RA   Hong T., Boo L.M., Wu H., Waring A.J., Lehrer R.I.;
RT   "SMAP-29 has two LPS-binding sites and a central hinge.";
RL   Eur. J. Biochem. 269:1181-1189(2002).
CC   -!- FUNCTION: Broad spectrum bactericidal agent.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR   EMBL; X92757; CAA63412.1; -; mRNA.
DR   EMBL; U60600; AAB49715.1; -; Genomic_DNA.
DR   PIR; S68411; S68411.
DR   PIR; S68412; S68412.
DR   PDB; 1FRY; NMR; -; A=132-160.
DR   PDB; 5Z26; NMR; -; A=132-149.
DR   PDBsum; 1FRY; -.
DR   PDBsum; 5Z26; -.
DR   AlphaFoldDB; P49928; -.
DR   BMRB; P49928; -.
DR   SMR; P49928; -.
DR   EvolutionaryTrace; P49928; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019835; P:cytolysis; IMP:AgBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:AgBase.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:AgBase.
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   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Disulfide bond;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..131
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004758"
FT   PEPTIDE         132..160
FT                   /note="Cathelin-related peptide SC5"
FT                   /id="PRO_0000004759"
FT   DISULFID        86..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..125
FT                   /evidence="ECO:0000250"
FT   STRAND          135..138
FT                   /evidence="ECO:0007829|PDB:1FRY"
FT   STRAND          141..144
FT                   /evidence="ECO:0007829|PDB:1FRY"
FT   TURN            145..148
FT                   /evidence="ECO:0007829|PDB:1FRY"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:1FRY"
FT   STRAND          153..158
FT                   /evidence="ECO:0007829|PDB:1FRY"
SQ   SEQUENCE   160 AA;  17786 MW;  BD9B3859C432C249 CRC64;
     METQRASLSL GRCSLWLLLL GLALPSASAQ VLSYREAVLR AADQLNEKSS EANLYRLLEL
     DPPPKQDDEN SNIPKPVSFR VKETVCPRTS QQPAEQCDFK ENGLLKECVG TVTLDQVRNN
     FDITCAEPQS VRGLRRLGRK IAHGVKKYGP TVLRIIRIAG