ACRBP_PIG
ID ACRBP_PIG Reviewed; 539 AA.
AC Q29016;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 2.
DT 03-AUG-2022, entry version 91.
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 AltName: Full=p32 {ECO:0000303|PubMed:15955892};
DE Flags: Precursor;
GN Name=ACRBP {ECO:0000250|UniProtKB:Q8NEB7};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA03737.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PROACROSIN, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, PROTEIN SEQUENCE OF 424-430, PROTEOLYTIC
RP CLEAVAGE, AND FUNCTION.
RC TISSUE=Testis {ECO:0000312|EMBL:BAA03737.1};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=15955892; DOI=10.2164/jandrol.04163;
RA Dube C., Leclerc P., Baba T., Reyes-Moreno C., Bailey J.L.;
RT "The proacrosin binding protein, sp32, is tyrosine phosphorylated during
RT capacitation of pig sperm.";
RL J. Androl. 26:519-528(2005).
CC -!- FUNCTION: [Acrosin-binding protein, mature form]: Acrosomal protein
CC that maintains proacrosin (pro-ACR) as an enzymatically inactive
CC zymogen in the acrosome (PubMed:8144514). Involved also in the acrosome
CC formation (By similarity). {ECO:0000250|UniProtKB:Q3V140,
CC ECO:0000269|PubMed:8144514}.
CC -!- SUBUNIT: [Acrosin-binding protein, mature form]: Binds specifically to
CC the 55- and 53-kDa proacrosins and the 49-kDa acrosin intermediate, but
CC is not capable of binding 43-kDa acrosin intermediate and 32-kDa mature
CC acrosin. {ECO:0000269|PubMed:8144514}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15955892,
CC ECO:0000269|PubMed:8144514}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000269|PubMed:15955892, ECO:0000269|PubMed:8144514}.
CC Note=Appears to be present only in the round spermatids and elongating
CC spermatids. Colocalizes in the acrosome with proacrosin.
CC {ECO:0000269|PubMed:8144514}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in testis.
CC {ECO:0000269|PubMed:8144514}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8144514}.
CC -!- PTM: Synthesized as a 60-kDa precursor, the 35-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:0000269|PubMed:8144514}.
CC -!- PTM: Phosphorylated on Tyr residues in capacitated sperm.
CC {ECO:0000269|PubMed:15955892}.
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DR EMBL; D16200; BAA03737.1; -; mRNA.
DR EMBL; AEMK02000037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A54424; A54424.
DR RefSeq; XP_003126581.1; XM_003126533.3.
DR AlphaFoldDB; Q29016; -.
DR STRING; 9823.ENSSSCP00000000746; -.
DR PaxDb; Q29016; -.
DR PeptideAtlas; Q29016; -.
DR Ensembl; ENSSSCT00000000762; ENSSSCP00000000746; ENSSSCG00000000700.
DR Ensembl; ENSSSCT00025037724; ENSSSCP00025015851; ENSSSCG00025027786.
DR Ensembl; ENSSSCT00030053689; ENSSSCP00030024505; ENSSSCG00030038486.
DR Ensembl; ENSSSCT00035110972; ENSSSCP00035048498; ENSSSCG00035080862.
DR Ensembl; ENSSSCT00040079975; ENSSSCP00040034585; ENSSSCG00040058660.
DR Ensembl; ENSSSCT00045025396; ENSSSCP00045017530; ENSSSCG00045014748.
DR Ensembl; ENSSSCT00050103889; ENSSSCP00050045501; ENSSSCG00050075715.
DR Ensembl; ENSSSCT00055060263; ENSSSCP00055048288; ENSSSCG00055030197.
DR Ensembl; ENSSSCT00060051882; ENSSSCP00060022078; ENSSSCG00060038315.
DR Ensembl; ENSSSCT00065108364; ENSSSCP00065048417; ENSSSCG00065078148.
DR Ensembl; ENSSSCT00070039850; ENSSSCP00070033376; ENSSSCG00070020101.
DR GeneID; 397317; -.
DR KEGG; ssc:397317; -.
DR CTD; 84519; -.
DR VGNC; VGNC:85029; ACRBP.
DR eggNOG; ENOG502R6TS; Eukaryota.
DR GeneTree; ENSGT00390000000826; -.
DR HOGENOM; CLU_534141_0_0_1; -.
DR InParanoid; Q29016; -.
DR OMA; CPLCAFC; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Proteomes; UP000314985; Chromosome 5.
DR Bgee; ENSSSCG00000000700; Expressed in testis and 41 other tissues.
DR ExpressionAtlas; Q29016; baseline and differential.
DR Genevisible; Q29016; SS.
DR GO; GO:0002080; C:acrosomal membrane; IDA:UniProtKB.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0035064; F:methylated histone binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0001675; P:acrosome assembly; ISS:UniProtKB.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IEA:Ensembl.
DR GO; GO:0006260; P:DNA replication; IEA:Ensembl.
DR GO; GO:0043966; P:histone H3 acetylation; IEA:Ensembl.
DR GO; GO:0043983; P:histone H4-K12 acetylation; IEA:Ensembl.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IEA:Ensembl.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045926; P:negative regulation of growth; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IEA:Ensembl.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IEA:Ensembl.
DR GO; GO:0048240; P:sperm capacitation; TAS:UniProtKB.
DR InterPro; IPR009865; Proacrosin-bd.
DR PANTHER; PTHR21362; PTHR21362; 1.
DR Pfam; PF07222; PBP_sp32; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..539
FT /note="Acrosin-binding protein"
FT /id="PRO_0000227518"
FT PROPEP 26..269
FT /note="Removed in active form"
FT /evidence="ECO:0000269|PubMed:8144514"
FT /id="PRO_0000449371"
FT CHAIN 270..539
FT /note="Acrosin-binding protein, mature form"
FT /evidence="ECO:0000269|PubMed:8144514"
FT /id="PRO_0000449372"
FT REGION 26..106
FT /note="Pro-ACR binding"
FT /evidence="ECO:0000250|UniProtKB:Q3V140"
FT REGION 186..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..423
FT /note="Pro-ACR binding"
FT /evidence="ECO:0000250|UniProtKB:Q3V140"
FT COMPBIAS 192..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 60827 MW; 82711EAB01C35F4F CRC64;
MRQLAAGSLL SLLKVLLLPL APAPAQDANS ASTPGSPLSP TEYERFFALL TPTWKAETTC
RLRATHGCRN PTLVQLDQYE NHGLVPDGAV CSDLPYASWF ESFCQFTQYR CSNHVYYAKR
VRCSQPVSIL SPNSLKEVDT SSEVPITTMT SPVSSHITAT GRQVFQPWPE RLNNNVEELL
QSSLSLGGQE QGQEHKQEHK QEQGQEHKQD EGQEQEEQEE EQEEEGKQEE GQGTEESLEA
MSGLQADSEP KFQSEFVSSN PFSFTPRVRE VESTPMMMEN IQELIRSAQE MDEMGDVYEE
ENIWRAQSPG SLLQLPHVDA LLVLCYSIVE NTCVITPTAK AWQYLEDETL GFGKSVCDSL
GRRHLAACSL CDFCSLKLEQ CHSETNLQRQ QCDNSHKTPF ISPLLASQSM SIGTQIGTLK
SGRFYGLDLY GGLRMDFWCA RLATKGCEDN RVASWLQTEF LSFQDGDFPT KICDTEYVQY
PNYCAFKSQQ CMMRNRDRKV SRMRCLQNET YTVLTQAKSE DLVLRWSQEF STLTLGQAG
