SACA1_HUMAN
ID SACA1_HUMAN Reviewed; 294 AA.
AC Q9HBV2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sperm acrosome membrane-associated protein 1;
DE AltName: Full=Sperm acrosomal membrane-associated protein 32;
DE Flags: Precursor;
GN Name=SPACA1; Synonyms=SAMP32;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 255-268, FUNCTION,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-256, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Testis;
RX PubMed=11870081; DOI=10.1095/biolreprod66.3.735;
RA Hao Z., Wolkowicz M.J., Shetty J., Klotz K., Bolling L., Sen B.,
RA Westbrook V.A., Coonrod S., Flickinger C.J., Herr J.C.;
RT "SAMP32, a testis-specific, isoantigenic sperm acrosomal membrane-
RT associated protein.";
RL Biol. Reprod. 66:735-744(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: Plays a role in acrosome expansion and establishment of
CC normal sperm morphology during spermatogenesis (By similarity).
CC Important for male fertility (PubMed:11870081).
CC {ECO:0000250|UniProtKB:Q9DA48, ECO:0000269|PubMed:11870081}.
CC -!- INTERACTION:
CC Q9HBV2; Q9NRZ5: AGPAT4; NbExp=3; IntAct=EBI-17498703, EBI-1754287;
CC Q9HBV2; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-17498703, EBI-3904417;
CC Q9HBV2; P27449: ATP6V0C; NbExp=3; IntAct=EBI-17498703, EBI-721179;
CC Q9HBV2; Q12983: BNIP3; NbExp=3; IntAct=EBI-17498703, EBI-749464;
CC Q9HBV2; P62955: CACNG7; NbExp=3; IntAct=EBI-17498703, EBI-17499011;
CC Q9HBV2; P21854: CD72; NbExp=3; IntAct=EBI-17498703, EBI-307924;
CC Q9HBV2; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-17498703, EBI-12256978;
CC Q9HBV2; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-17498703, EBI-12019274;
CC Q9HBV2; P54849: EMP1; NbExp=3; IntAct=EBI-17498703, EBI-4319440;
CC Q9HBV2; P54852: EMP3; NbExp=3; IntAct=EBI-17498703, EBI-3907816;
CC Q9HBV2; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-17498703, EBI-6166686;
CC Q9HBV2; Q8N112: LSMEM2; NbExp=3; IntAct=EBI-17498703, EBI-10264855;
CC Q9HBV2; Q8IZ57: NRSN1; NbExp=3; IntAct=EBI-17498703, EBI-10264528;
CC Q9HBV2; P42857: NSG1; NbExp=3; IntAct=EBI-17498703, EBI-6380741;
CC Q9HBV2; P26678: PLN; NbExp=3; IntAct=EBI-17498703, EBI-692836;
CC Q9HBV2; Q01453: PMP22; NbExp=3; IntAct=EBI-17498703, EBI-2845982;
CC Q9HBV2; Q9NS64: RPRM; NbExp=3; IntAct=EBI-17498703, EBI-1052363;
CC Q9HBV2; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-17498703, EBI-749270;
CC Q9HBV2; A2A2V5: SERTM1; NbExp=3; IntAct=EBI-17498703, EBI-17284533;
CC Q9HBV2; Q13326: SGCG; NbExp=3; IntAct=EBI-17498703, EBI-5357343;
CC Q9HBV2; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-17498703, EBI-10226799;
CC Q9HBV2; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-17498703, EBI-741850;
CC Q9HBV2; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-17498703, EBI-17192156;
CC Q9HBV2; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-17498703, EBI-2844246;
CC Q9HBV2; Q9BQJ4: TMEM47; NbExp=3; IntAct=EBI-17498703, EBI-13370320;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC inner membrane {ECO:0000269|PubMed:11870081}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=Primarily found in the equatorial
CC segment of the acrosome (PubMed:11870081). The tyrosine phosphorylated
CC protein localizes to a smaller region within the equatorial segment (By
CC similarity). Also expressed weakly in the principal segment
CC (PubMed:11870081). {ECO:0000250|UniProtKB:D5K8A9,
CC ECO:0000269|PubMed:11870081}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11870081}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9DA48}.
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DR EMBL; AF203447; AAG31422.1; -; mRNA.
DR EMBL; AL136096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029488; AAH29488.1; -; mRNA.
DR CCDS; CCDS5014.1; -.
DR RefSeq; NP_112222.1; NM_030960.2.
DR AlphaFoldDB; Q9HBV2; -.
DR BioGRID; 123591; 116.
DR IntAct; Q9HBV2; 73.
DR MINT; Q9HBV2; -.
DR STRING; 9606.ENSP00000237201; -.
DR GlyGen; Q9HBV2; 1 site.
DR iPTMnet; Q9HBV2; -.
DR PhosphoSitePlus; Q9HBV2; -.
DR BioMuta; SPACA1; -.
DR DMDM; 74752784; -.
DR MassIVE; Q9HBV2; -.
DR PaxDb; Q9HBV2; -.
DR PeptideAtlas; Q9HBV2; -.
DR PRIDE; Q9HBV2; -.
DR ProteomicsDB; 81599; -.
DR Antibodypedia; 18684; 125 antibodies from 21 providers.
DR DNASU; 81833; -.
DR Ensembl; ENST00000237201.2; ENSP00000237201.1; ENSG00000118434.9.
DR GeneID; 81833; -.
DR KEGG; hsa:81833; -.
DR MANE-Select; ENST00000237201.2; ENSP00000237201.1; NM_030960.3; NP_112222.1.
DR UCSC; uc003pmn.3; human.
DR CTD; 81833; -.
DR DisGeNET; 81833; -.
DR GeneCards; SPACA1; -.
DR HGNC; HGNC:14967; SPACA1.
DR HPA; ENSG00000118434; Tissue enriched (testis).
DR MIM; 612739; gene.
DR neXtProt; NX_Q9HBV2; -.
DR OpenTargets; ENSG00000118434; -.
DR PharmGKB; PA37943; -.
DR VEuPathDB; HostDB:ENSG00000118434; -.
DR eggNOG; ENOG502S339; Eukaryota.
DR GeneTree; ENSGT00390000004211; -.
DR HOGENOM; CLU_080745_0_0_1; -.
DR InParanoid; Q9HBV2; -.
DR OMA; FIIVNWA; -.
DR OrthoDB; 1279146at2759; -.
DR PhylomeDB; Q9HBV2; -.
DR TreeFam; TF336918; -.
DR PathwayCommons; Q9HBV2; -.
DR SignaLink; Q9HBV2; -.
DR BioGRID-ORCS; 81833; 9 hits in 1060 CRISPR screens.
DR ChiTaRS; SPACA1; human.
DR GenomeRNAi; 81833; -.
DR Pharos; Q9HBV2; Tbio.
DR PRO; PR:Q9HBV2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9HBV2; protein.
DR Bgee; ENSG00000118434; Expressed in left testis and 27 other tissues.
DR Genevisible; Q9HBV2; HS.
DR GO; GO:0002080; C:acrosomal membrane; IBA:GO_Central.
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..294
FT /note="Sperm acrosome membrane-associated protein 1"
FT /id="PRO_0000248152"
FT TOPO_DOM 30..221
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 42..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11870081"
FT MOD_RES 269
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D5K8A9"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DA48"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 237
FT /note="L -> S (in dbSNP:rs2276089)"
FT /id="VAR_027258"
SQ SEQUENCE 294 AA; 32143 MW; 60DB3107E1B03D12 CRC64;
MSPRGTGCSA GLLMTVGWLL LAGLQSARGT NVTAAVQDAG LAHEGEGEEE TENNDSETAE
NYAPPETEDV SNRNVVKEVE FGMCTVTCGI GVREVILTNG CPGGESKCVV RVEECRGPTD
CGWGKPISES LESVRLACIH TSPLNRFKYM WKLLRQDQQS IILVNDSAIL EVRKESHPLA
FECDTLDNNE IVATIKFTVY TSSELQMRRS SLPATDAALI FVLTIGVIIC VFIIFLLIFI
IINWAAVKAF WGAKASTPEV QSEQSSVRYK DSTSLDQLPT EMPGEDDALS EWNE
