ID   SPBP_RAT                Reviewed;         279 AA.
AC   P08723;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Prostatic spermine-binding protein;
DE            Short=SBP;
DE   Flags: Precursor;
GN   Name=Sbp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3818623; DOI=10.1016/s0021-9258(18)61581-9;
RA   Chang C., Saltzman A.G., Hiipakka R.A., Huang I.-Y., Liao S.;
RT   "Prostatic spermine-binding protein. Cloning and nucleotide sequence of
RT   cDNA, amino acid sequence, and androgenic control of mRNA level.";
RL   J. Biol. Chem. 262:2826-2831(1987).
RN   [2]
RP   PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-18, AND SEQUENCE REVISION.
RX   PubMed=3166977; DOI=10.1021/bi00412a002;
RA   Anderegg R.J., Carr S.A., Huang I.-Y., Hiipakka R.A., Chang C., Liao S.;
RT   "Correction of the cDNA-derived protein sequence of prostatic spermine
RT   binding protein: pivotal role of tandem mass spectrometry in sequence
RT   analysis.";
RL   Biochemistry 27:4214-4221(1988).
CC   -!- FUNCTION: Spermine-binding protein is an androgen regulated ventral
CC       prostate glycoprotein that binds various polyamines.
CC   -!- TISSUE SPECIFICITY: Prostate.
CC   -!- SIMILARITY: To mouse SBP. {ECO:0000305}.
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DR   EMBL; J02675; AAA42113.1; ALT_SEQ; mRNA.
DR   PIR; A28714; A28714.
DR   PIR; A29561; A29561.
DR   AlphaFoldDB; P08723; -.
DR   SMR; P08723; -.
DR   STRING; 10116.ENSRNOP00000065825; -.
DR   GlyGen; P08723; 1 site.
DR   PRIDE; P08723; -.
DR   UCSC; RGD:3623; rat.
DR   RGD; 3623; Sbp.
DR   InParanoid; P08723; -.
DR   PRO; PR:P08723; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0019808; F:polyamine binding; TAS:RGD.
DR   Gene3D; 2.100.10.30; -; 1.
DR   InterPro; IPR001229; Jacalin-like_lectin_dom.
DR   InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR   Pfam; PF01419; Jacalin; 1.
DR   SMART; SM00915; Jacalin; 1.
DR   SUPFAM; SSF51101; SSF51101; 1.
DR   PROSITE; PS51752; JACALIN_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Lectin;
KW   Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT   SIGNAL          1..17
FT   CHAIN           18..279
FT                   /note="Prostatic spermine-binding protein"
FT                   /id="PRO_0000022390"
FT   DOMAIN          18..151
FT                   /note="Jacalin-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT   REGION          160..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..179
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..279
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:3166977"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
SQ   SEQUENCE   279 AA;  31080 MW;  3BEB01A02A517A65 CRC64;
     MLLLVTLALL AGPTCRAQNI LGNNVGTYFY VAGEEHGQLR GIRIFLTVID LIKGIQLRFG
     GNWSDVYGSR SLKYKEFLLE DGEHVTQVSG TRKLCLTSLS FTTNKGRVVT FGVRRGLSFN
     ESGGSDKYLV TVNGLYAPGL CLNGMGFKWK NIHDDFDDND DDKEDDDDEH DDDNEEDHGD
     KDNDNDHDDD HDDDDDDKED DNEEDVDDER DDKDDDEEDD DNDKENDKDD GEGSGDDDDN
     DDEDDDKDDD GGSGDDGDDG DDDEDDDGGD DDNGDEEEE