ID   P15B_RABIT              Reviewed;         137 AA.
AC   P26203;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=15 kDa protein B;
DE   AltName: Full=P15H;
DE   AltName: Full=Protein P15B;
DE   Flags: Precursor;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Bone marrow;
RX   PubMed=8449963; DOI=10.1016/s0021-9258(18)53425-6;
RA   Levy O., Weiss J., Zarember K., Ooi C.E., Elsbach P.;
RT   "Antibacterial 15-kDa protein isoforms (p15s) are members of a novel family
RT   of leukocyte proteins.";
RL   J. Biol. Chem. 268:6058-6063(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8273570; DOI=10.1007/bf01972768;
RA   Levy O., Weiss J., Ooi C.E., Elsbach P.;
RT   "Structural characterization of BPI-modulating 15 kDa proteins from rabbit
RT   polymorphonuclear leukocytes: identification of a novel family of leukocyte
RT   proteins.";
RL   Agents Actions 39:C207-C210(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-40.
RC   TISSUE=Neutrophil;
RX   PubMed=2203792; DOI=10.1016/s0021-9258(18)55490-9;
RA   Ooi C.E., Weiss J., Levy O., Elsbach P.;
RT   "Isolation of two isoforms of a novel 15-kDa protein from rabbit
RT   polymorphonuclear leukocytes that modulate the antibacterial actions of
RT   other leukocyte proteins.";
RL   J. Biol. Chem. 265:15956-15962(1990).
CC   -!- FUNCTION: Binds to bacterial lipopolysaccharides (LPS), potentiates
CC       weakly the early antibacterial effects of BPI. Inhibits the late lethal
CC       action of BPI.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Large granules of neutrophils.
CC   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR   EMBL; L07587; AAA99903.1; ALT_SEQ; mRNA.
DR   EMBL; S68155; AAB29404.1; -; mRNA.
DR   PIR; B46634; B46634.
DR   AlphaFoldDB; P26203; -.
DR   SMR; P26203; -.
DR   Proteomes; UP000001811; 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   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:2203792"
FT   CHAIN           21..137
FT                   /note="15 kDa protein B"
FT                   /id="PRO_0000004757"
FT   DISULFID        77..88
FT                   /evidence="ECO:0000250"
FT   DISULFID        99..116
FT                   /evidence="ECO:0000250"
FT   CONFLICT        39
FT                   /note="Y -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   137 AA;  15626 MW;  CD06B1FA139E79B2 CRC64;
     MAGVWKVLVV LVGLAVVACA IPHRRLRYEE VVAQALQFYN EGQQGQPLFR LLEATPPPSL
     NSKSRIPLNF RIKETVCIFT LDRQPGNCAF REGGEERICR GAFVRRRRVR ALTLRCDRDQ
     RRQPEFPRVT RPAGPTA