SACA1_PIG
ID SACA1_PIG Reviewed; 295 AA.
AC D5K8A9;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Sperm acrosome membrane-associated protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=SPACA1 {ECO:0000303|PubMed:18448843};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|Proteomes:UP000008227};
RN [1] {ECO:0000312|EMBL:ADE28547.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu Y.G.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000008227}
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 PROTEIN SEQUENCE OF 259-270, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PHOSPHORYLATION AT SER-256; TYR-269 AND SER-278, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18448843; DOI=10.1095/biolreprod.107.067314;
RA Jones R., James P.S., Oxley D., Coadwell J., Suzuki-Toyota F., Howes E.A.;
RT "The equatorial subsegment in mammalian spermatozoa is enriched in tyrosine
RT phosphorylated proteins.";
RL Biol. Reprod. 79:421-431(2008).
CC -!- FUNCTION: Plays a role in acrosome expansion and establishment of
CC normal sperm morphology during spermatogenesis. Important for male
CC fertility. {ECO:0000250|UniProtKB:Q9DA48}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC inner membrane {ECO:0000269|PubMed:18448843}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=Primarily found in the equatorial
CC segment of the acrosome (PubMed:18448843). The tyrosine phosphorylated
CC protein localizes to a smaller region within the equatorial segment
CC (PubMed:18448843). Also expressed weakly in the principal segment (By
CC similarity). {ECO:0000250|UniProtKB:Q9HBV2,
CC ECO:0000269|PubMed:18448843}.
CC -!- TISSUE SPECIFICITY: Detected in spermatozoa (at protein level).
CC {ECO:0000269|PubMed:18448843}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9DA48}.
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DR EMBL; GU475011; ADE28547.1; -; mRNA.
DR EMBL; AEMK02000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001177176.1; NM_001190247.1.
DR AlphaFoldDB; D5K8A9; -.
DR STRING; 9823.ENSSSCP00000004652; -.
DR iPTMnet; D5K8A9; -.
DR PaxDb; D5K8A9; -.
DR PeptideAtlas; D5K8A9; -.
DR PRIDE; D5K8A9; -.
DR Ensembl; ENSSSCT00000004763; ENSSSCP00000004652; ENSSSCG00000004308.
DR Ensembl; ENSSSCT00005040899; ENSSSCP00005025025; ENSSSCG00005025757.
DR Ensembl; ENSSSCT00015049687; ENSSSCP00015019800; ENSSSCG00015037247.
DR Ensembl; ENSSSCT00025088606; ENSSSCP00025038717; ENSSSCG00025064612.
DR Ensembl; ENSSSCT00030079649; ENSSSCP00030036468; ENSSSCG00030057130.
DR Ensembl; ENSSSCT00035096990; ENSSSCP00035040897; ENSSSCG00035071702.
DR Ensembl; ENSSSCT00045049085; ENSSSCP00045034150; ENSSSCG00045028778.
DR Ensembl; ENSSSCT00050103399; ENSSSCP00050045211; ENSSSCG00050075410.
DR Ensembl; ENSSSCT00055006203; ENSSSCP00055004871; ENSSSCG00055003198.
DR Ensembl; ENSSSCT00060069835; ENSSSCP00060030106; ENSSSCG00060051315.
DR Ensembl; ENSSSCT00065082802; ENSSSCP00065036079; ENSSSCG00065060441.
DR Ensembl; ENSSSCT00070049306; ENSSSCP00070041650; ENSSSCG00070024706.
DR GeneID; 100156797; -.
DR KEGG; ssc:100156797; -.
DR CTD; 81833; -.
DR VGNC; VGNC:93367; SPACA1.
DR eggNOG; ENOG502S339; Eukaryota.
DR GeneTree; ENSGT00390000004211; -.
DR HOGENOM; CLU_080745_0_0_1; -.
DR InParanoid; D5K8A9; -.
DR OMA; FIIVNWA; -.
DR OrthoDB; 1279146at2759; -.
DR TreeFam; TF336918; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000004308; Expressed in testis and 12 other tissues.
DR GO; GO:0002080; C:acrosomal membrane; IDA:UniProtKB.
DR GO; GO:0002079; C:inner acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001675; P:acrosome assembly; IBA:GO_Central.
DR CDD; cd13783; SPACA1; 1.
DR InterPro; IPR037878; SPACA1.
DR PANTHER; PTHR47223; PTHR47223; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..295
FT /note="Sperm acrosome membrane-associated protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5011205355"
FT TOPO_DOM 30..220
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 39..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..64
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18448843"
FT MOD_RES 269
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18448843"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18448843"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DA48"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 295 AA; 32239 MW; 00DF8A789FC329D7 CRC64;
MSPGGAGCSA GLLLTVGWLL LAGLQSTCGI NVTAVQDPSL VSEGENEGEE EAENDSEVEN
EPQAEAEQDV SNKTVVKEVE FGMCTVTCGV GIREVLLTNG CPGGESKCIV RVEECRGPVD
CGWGKPISEN LESVRLSCVH TSPVNRFKYV WRLLRPNQQA VILANDSAIL EVQRETHPMA
FQCETLDNNE IVATVKFTVY TTAELQMKRS SRPDTDAVLV FVLTIGVIIC IFVIFVLIFI
IVNWATVKDF WASKASTTEI QSELSSMKYK DSTSLDQSPT EIPGHEDDAL SEWNE
