ASPX_VULVU
ID ASPX_VULVU Reviewed; 349 AA.
AC P53353;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Sperm acrosomal protein FSA-ACR.1;
DE Flags: Precursor; Fragment;
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Testis;
RX PubMed=7766418; DOI=10.1002/mrd.1080400214;
RA Beaton S., ten Have J., Cleary A., Bradley M.P.;
RT "Cloning and partial characterization of the cDNA encoding the fox sperm
RT protein FSA-Acr.1 with similarities to the SP-10 antigen.";
RL Mol. Reprod. Dev. 40:242-252(1995).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome.
CC Note=Intracellular acrosomal compartment of sperm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=FSA-Acr.1;
CC IsoId=P53353-1; Sequence=Displayed;
CC Name=2; Synonyms=FSA-Acr.2;
CC IsoId=P53353-2; Sequence=VSP_004130, VSP_004131;
CC Name=3; Synonyms=FSA-Acr.3;
CC IsoId=P53353-3; Sequence=VSP_004132;
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- SIMILARITY: To acrosomal proteins SP-10. {ECO:0000305}.
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DR EMBL; U06077; AAC48463.1; -; mRNA.
DR AlphaFoldDB; P53353; -.
DR STRING; 9627.ENSVVUP00000027517; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR CDD; cd00117; LU; 1.
DR InterPro; IPR016054; LY6_UPA_recep-like.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasmic vesicle; Glycoprotein;
KW Reference proteome; Repeat; Signal.
FT SIGNAL <1..8
FT /evidence="ECO:0000255"
FT CHAIN 9..349
FT /note="Sperm acrosomal protein FSA-ACR.1"
FT /id="PRO_0000020763"
FT REGION 1..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ <1..7
FT /note="MKEVYLV -> MSLYLI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7766418"
FT /id="VSP_004130"
FT VAR_SEQ 140
FT /note="G -> GEQPSGEKSSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7766418"
FT /id="VSP_004131"
FT VAR_SEQ 140
FT /note="G -> GEQPSGEKSLGEQPSGEKSSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7766418"
FT /id="VSP_004132"
FT NON_TER 1
SQ SEQUENCE 349 AA; 36486 MW; 10E762D86805BD83 CRC64;
MKEVYLVGYA RGASGQSDEP PGSMDHQASV QRLSGEYFSL GNPSDGEALY ETAAGENTLS
EHTSGEHTSV EHASAEHSST EHTSGEHASG EHTSGERATG EHTSSEHATS EHTSGEQPSG
EQPSGEKSSG EQPSGEKSSG EQPSGEKSLG EQPSGEQSSG EKSSAEQTSG EQAVAEKPSG
EHAVAEKPSG EQAVAERPSG EQAVAEKPLG EQAVAERPSG EQASIEKASS EQASAEQASA
EQASSEQASG EKPLGEQPSG IPPSSTFSGP ILNCHTCSYM NDQGKCLRGE GVCSTQNSQQ
CMLKKIFEGG KLQFMVQGCE NMCPSMNLFS HGTRMQIICC RNQSFCNKI