ACRBP_RAT
ID ACRBP_RAT Reviewed; 540 AA.
AC Q6AY33;
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 Flags: Precursor;
GN Name=Acrbp {ECO:0000312|EMBL:AAH79212.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acrosomal protein that maintains proacrosin (pro-ACR) as an
CC enzymatically inactive zymogen in the acrosome. Involved also in the
CC acrosome formation. {ECO:0000250|UniProtKB:Q3V140}.
CC -!- FUNCTION: [Acrosin-binding protein, mature form]: Maintains pro-ACR as
CC an enzymatically inactive zymogen in the acrosome until acrosomal
CC exocytosis. Partially contributes also to the assembly of acrosomal
CC proteins to form an acrosomal granule. {ECO:0000250|UniProtKB:Q3V140}.
CC -!- FUNCTION: [Isoform 2]: Rodent specific isoform that participates in the
CC formation of the acrosomal granule into the center of the acrosomal
CC vesicle during early spermiogenesis. In the fertilization process
CC promotes ACR release from the acrosome during acrosomal exocytosis.
CC {ECO:0000250|UniProtKB:Q3V140}.
CC -!- SUBUNIT: [Acrosin-binding protein, mature form]: Binds pro-ACR. Does
CC not bind the mature form of ACR. {ECO:0000250|UniProtKB:Q3V140}.
CC -!- SUBUNIT: [Isoform 2]: Binds pro-ACR. Does not bind mature form of ACR.
CC {ECO:0000250|UniProtKB:Q3V140}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory
CC vesicle, acrosome {ECO:0000250|UniProtKB:Q3V140}. Note=Colocalized with
CC pro-ACR in the acrosomal granules of early round spermatids.
CC {ECO:0000250|UniProtKB:Q3V140}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle, secretory
CC vesicle, acrosome {ECO:0000250|UniProtKB:Q3V140}. Note=Highly enriched
CC in acrosomal granules of round spermatids, and spread over the apical
CC end of the nucleus in elongating spermatids. Colocalized in the
CC acrosome of epididymal sperm with pro-ACR.
CC {ECO:0000250|UniProtKB:Q3V140}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6AY33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AY33-2; Sequence=VSP_060553, VSP_060554;
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; AC115415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC079212; AAH79212.1; -; mRNA.
DR RefSeq; NP_001020220.1; NM_001025049.1. [Q6AY33-2]
DR RefSeq; XP_006237441.1; XM_006237379.3. [Q6AY33-1]
DR AlphaFoldDB; Q6AY33; -.
DR STRING; 10116.ENSRNOP00000024618; -.
DR PaxDb; Q6AY33; -.
DR GeneID; 500316; -.
DR KEGG; rno:500316; -.
DR UCSC; RGD:1564880; rat. [Q6AY33-1]
DR CTD; 84519; -.
DR RGD; 1564880; Acrbp.
DR VEuPathDB; HostDB:ENSRNOG00000017399; -.
DR eggNOG; ENOG502R6TS; Eukaryota.
DR HOGENOM; CLU_879871_0_0_1; -.
DR InParanoid; Q6AY33; -.
DR OMA; VENSCSM; -.
DR OrthoDB; 961418at2759; -.
DR PhylomeDB; Q6AY33; -.
DR PRO; PR:Q6AY33; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000017399; Expressed in testis and 19 other tissues.
DR Genevisible; Q6AY33; RN.
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; IPR009865; Proacrosin-bd.
DR PANTHER; PTHR21362; PTHR21362; 1.
DR Pfam; PF07222; PBP_sp32; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasmic vesicle; Phosphoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..540
FT /note="Acrosin-binding protein"
FT /id="PRO_0000227519"
FT PROPEP 25..272
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q29016"
FT /id="PRO_0000449373"
FT CHAIN 273..316
FT /note="Acrosin-binding protein, mature form"
FT /id="PRO_0000449374"
FT REGION 25..104
FT /note="Pro-ACR binding"
FT /evidence="ECO:0000250|UniProtKB:Q3V140"
FT REGION 181..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..424
FT /note="Pro-ACR binding"
FT /evidence="ECO:0000250|UniProtKB:Q3V140"
FT COMPBIAS 194..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 312..316
FT /note="SLQQL -> RYRKL (in isoform 2)"
FT /id="VSP_060553"
FT VAR_SEQ 317..540
FT /note="Missing (in isoform 2)"
FT /id="VSP_060554"
SQ SEQUENCE 540 AA; 61080 MW; 27EEE0291175BBCE CRC64;
MKLAASFLLM LLEVLLLPET PLSAEEALAS TPGSPLSSTE YERFFALLTP TWKAETTCRL
RATHGCRNPT LVQLDQYENH GLVPDGAVCS DLPYASWFES FCQFAQYRCS NHVYYAKRVR
CSQPVSILSP NTLKEVESSA EVPLTSVTTP IVSRATATEH QAFQPWPERL NNNVEELLQS
SLSLGGKEQQ SSRKLGLEQQ HKQEQIQEHK LEEAQEQEEQ EEEEEEEEAK QEEGQGTEEG
LDSVSRLQSD SEPKFQSKSL SSNPSFFTPR VREVESAPLM MENIQELIRS AQEMDEMNEL
YDDSWRSQST GSLQQLPHTE TLMVLCYSIM ENTCTMTPTA KAWSYMEEEI LGFGDSVCDN
LGRRHTAACP LCAFCSLKLE QCHSEASVLR QQCDASHKIP FISPLLSAQS ISTGNQAKIP
EKGRFAGLEM YGGLSSEFWC NRLALKGCED DRVANWLKAE FLSFQDGDLP TKICDTNYVQ
YPNYCSFKSQ QCLLKNQNRK MSRMKCMLNE KYHVLSPAKG EEVILRWSQE FNTLTLGQFG
