ID   ACRBP_CAVPO             Reviewed;         543 AA.
AC   Q60485;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Acrosin-binding protein;
DE   AltName: Full=Acrosin-binding protein, 60 kDa form;
DE   AltName: Full=Proacrosin-binding protein sp32;
DE   Contains:
DE     RecName: Full=Acrosin-binding protein, mature form;
DE     AltName: Full=Acrosin-binding protein, 32 kDa form, mature form;
DE     AltName: Full=Sp32 {ECO:0000303|PubMed:8144514};
DE   Flags: Precursor;
GN   Name=ACRBP;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAA03740.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis {ECO:0000312|EMBL:BAA03740.1};
RX   PubMed=8144514; DOI=10.1016/s0021-9258(17)37000-x;
RA   Baba T., Niida Y., Michikawa Y., Kashiwabara S., Kodaira K., Takenaka M.,
RA   Kohno N., Gerton G.L., Arai Y.;
RT   "An acrosomal protein, sp32, mammalian sperm is a binding protein specific
RT   for two proacrosins and an acrosin intermediate.";
RL   J. Biol. Chem. 269:10133-10140(1994).
CC   -!- FUNCTION: [Acrosin-binding protein, mature form]: Acrosomal protein
CC       that maintains proacrosin (pro-ACR) as an enzymatically inactive
CC       zymogen in the acrosome. Involved also in the acrosome formation.
CC       {ECO:0000250|UniProtKB:Q3V140}.
CC   -!- SUBUNIT: [Acrosin-binding protein, mature form]: Binds proacrosin
CC       (ACR). Does not bind the mature form of ACR.
CC       {ECO:0000250|UniProtKB:Q29016}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q29016}.
CC       Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000250|UniProtKB:Q29016, ECO:0000250|UniProtKB:Q3V140}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in testis.
CC       {ECO:0000269|PubMed:8144514}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q29016}.
CC   -!- PTM: Phosphorylated on Tyr residues in capacitated sperm.
CC       {ECO:0000250|UniProtKB:Q29016}.
CC   -!- PTM: Synthesized as a 60-kDa precursor, the 32-kDa mature form is post-
CC       translationally produced by the removal of the N-terminal half of the
CC       precursor during sperm maturation in the testis and/or epididymis.
CC       {ECO:0000250|UniProtKB:Q29016}.
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DR   EMBL; D16203; BAA03740.1; -; mRNA.
DR   PIR; B54424; B54424.
DR   RefSeq; NP_001166378.1; NM_001172907.1.
DR   AlphaFoldDB; Q60485; -.
DR   STRING; 10141.ENSCPOP00000011063; -.
DR   GeneID; 100135468; -.
DR   KEGG; cpoc:100135468; -.
DR   CTD; 84519; -.
DR   eggNOG; ENOG502R6TS; Eukaryota.
DR   InParanoid; Q60485; -.
DR   OrthoDB; 961418at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0001675; P:acrosome assembly; ISS:UniProtKB.
DR   GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR009865; Proacrosin-bd.
DR   PANTHER; PTHR21362; PTHR21362; 1.
DR   Pfam; PF07222; PBP_sp32; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..543
FT                   /note="Acrosin-binding protein"
FT                   /id="PRO_0000227515"
FT   PROPEP          26..276
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q29016"
FT                   /id="PRO_0000449365"
FT   CHAIN           277..543
FT                   /note="Acrosin-binding protein, mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q29016"
FT                   /id="PRO_0000449366"
FT   REGION          26..106
FT                   /note="Pro-ACR binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q3V140"
FT   REGION          187..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..427
FT                   /note="Pro-ACR binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q3V140"
FT   COMPBIAS        197..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..235
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  61202 MW;  B8BBFB34EB87A50F CRC64;
     MGQPAAGSIL TLLRVLLLPL GPALAQDSPS APTPGSPLSP TEYERFFALL TPTWKAETTC
     RLRATHGCRN PTIVQLDQYE NHGLVPDGAV CSDLPYASWF ESFCQFSQYR CSNHVYYAKR
     VRCSQPVSIL SVNSFKELES PVEVSPTTMT SPVTSHIKAT ERQSFQAWPE RLSNNVEELL
     QSSLSLAGQE QAAGHKQEQG QEQHKQDPTQ EHKQDDGQEQ EEQEEEQEEE GKQEEGQSVE
     DMLGRVGRAG LRIGSEPKPQ SLSLSSDPHS FTARVRDVDS APMMIENIQE LIQSAQEMEE
     MYEEDAYWRS QNHGSLLQLP HKEALLVLCY SIVMNSCVMT PSAKAWKYLE EETFGFGKSV
     CDNLGRRHMA LCPLCAFCSL KLEQCHSEAN LQRQQCDASH KTPFISSLLT AQTMSMGTQA
     GTSESGRFYG LDVYGGLRMD FWCARLATKG CEDIRVSSWL QTEFLSFHNG DFPTKVCDTD
     YIQYPNYCSF KSQQCLMKNR NRKVSRMRCM QNETYNVLTP SKGEDLVLRW SQEFSTLALS
     RFG