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SACA3_HUMAN
ID   SACA3_HUMAN             Reviewed;         215 AA.
AC   Q8IXA5; Q7Z4Y5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Sperm acrosome membrane-associated protein 3;
DE   AltName: Full=Cancer/testis antigen 54;
DE            Short=CT54;
DE   AltName: Full=Lysozyme-like acrosomal sperm-specific secretory protein ALLP-17;
DE   AltName: Full=Lysozyme-like protein 3;
DE   AltName: Full=Sperm lysozyme-like protein 1;
DE   AltName: Full=Sperm protein reactive with antisperm antibodies;
DE            Short=Sperm protein reactive with ASA;
DE   Contains:
DE     RecName: Full=Sperm acrosome membrane-associated protein 3, membrane form;
DE   Contains:
DE     RecName: Full=Sperm acrosome membrane-associated protein 3, processed form;
GN   Name=SPACA3; Synonyms=LYC3, LYZL3, SLLP1, SPRASA; ORFNames=UNQ424/PRO862;
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] (ISOFORM 1), PROTEIN SEQUENCE OF 88-109,
RP   FUNCTION IN FERTILIZATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=12606493; DOI=10.1095/biolreprod.102.010108;
RA   Mandal A., Klotz K.L., Shetty J., Jayes F.L., Wolkowicz M.J., Bolling L.C.,
RA   Coonrod S.A., Black M.B., Diekman A.B., Haystead T.A.J., Flickinger C.J.,
RA   Herr J.C.;
RT   "SLLP1, a unique, intra-acrosomal, non-bacteriolytic, c lysozyme-like
RT   protein of human spermatozoa.";
RL   Biol. Reprod. 68:1525-1537(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=16014814; DOI=10.1095/biolreprod.105.041889;
RA   Zhang K., Gao R., Zhang H., Cai X., Shen C., Wu C., Zhao S., Yu L.;
RT   "Molecular cloning and characterization of three novel lysozyme-like genes,
RT   predominantly expressed in the male reproductive system of humans,
RT   belonging to the c-type lysozyme/alpha-lactalbumin family.";
RL   Biol. Reprod. 73:1064-1071(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Sperm;
RX   PubMed=14747161; DOI=10.1093/humrep/deh050;
RA   Chiu W.W.C., Erikson E.K., Sole C.A., Shelling A.N., Chamley L.W.;
RT   "SPRASA, a novel sperm protein involved in immune-mediated infertility.";
RL   Hum. Reprod. 19:243-249(2004).
CC   -!- FUNCTION: Sperm surface membrane protein that may be involved in sperm-
CC       egg plasma membrane adhesion and fusion during fertilization. It could
CC       be a potential receptor for the egg oligosaccharide residue N-
CC       acetylglucosamine, which is present in the extracellular matrix over
CC       the egg plasma membrane. The processed form has no detectable
CC       bacteriolytic activity in vitro. {ECO:0000269|PubMed:12606493}.
CC   -!- SUBUNIT: Interacts with ASTL. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory
CC       vesicle, acrosome membrane {ECO:0000305}; Single-pass type II membrane
CC       protein {ECO:0000305}. Note=Anterior acrosome in non-capacitated
CC       spermatozoa and retained in the equatorial segment and in the luminal
CC       face of both the inner and outer acrosomal membranes following
CC       capacitation and the acrosome reaction. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IXA5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IXA5-2; Sequence=VSP_021329;
CC   -!- TISSUE SPECIFICITY: The processed form is expressed in sperm (at
CC       protein level). Expressed in testis, epididymis and placenta.
CC       {ECO:0000269|PubMed:12606493, ECO:0000269|PubMed:16014814}.
CC   -!- PTM: The processed form derives from the membrane form by proteolytic
CC       processing.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC   -!- CAUTION: Although it belongs to the glycosyl hydrolase 22 family, Thr-
CC       122 and Asn-139 are present instead of the conserved Glu and Asp which
CC       are active site residues. It is therefore expected that this protein
CC       lacks hydrolase activity. {ECO:0000305}.
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DR   EMBL; AF216311; AAK01478.1; -; mRNA.
DR   EMBL; AF099029; AAP97222.1; -; Genomic_DNA.
DR   EMBL; AY358653; AAQ89016.1; -; mRNA.
DR   EMBL; BC100886; AAI00887.1; -; mRNA.
DR   EMBL; BC100887; AAI00888.1; -; mRNA.
DR   CCDS; CCDS11275.1; -. [Q8IXA5-1]
DR   RefSeq; NP_001304155.1; NM_001317226.1.
DR   RefSeq; NP_776246.1; NM_173847.4. [Q8IXA5-1]
DR   AlphaFoldDB; Q8IXA5; -.
DR   SMR; Q8IXA5; -.
DR   BioGRID; 125897; 29.
DR   IntAct; Q8IXA5; 7.
DR   STRING; 9606.ENSP00000269053; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   GlyGen; Q8IXA5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8IXA5; -.
DR   PhosphoSitePlus; Q8IXA5; -.
DR   BioMuta; SPACA3; -.
DR   DMDM; 74723659; -.
DR   MassIVE; Q8IXA5; -.
DR   PaxDb; Q8IXA5; -.
DR   PeptideAtlas; Q8IXA5; -.
DR   PRIDE; Q8IXA5; -.
DR   ProteomicsDB; 70978; -. [Q8IXA5-1]
DR   ProteomicsDB; 70979; -. [Q8IXA5-2]
DR   Antibodypedia; 15460; 71 antibodies from 20 providers.
DR   DNASU; 124912; -.
DR   Ensembl; ENST00000269053.8; ENSP00000269053.3; ENSG00000141316.13. [Q8IXA5-1]
DR   Ensembl; ENST00000580599.5; ENSP00000463386.1; ENSG00000141316.13. [Q8IXA5-2]
DR   GeneID; 124912; -.
DR   KEGG; hsa:124912; -.
DR   MANE-Select; ENST00000269053.8; ENSP00000269053.3; NM_173847.5; NP_776246.1.
DR   UCSC; uc002hhs.2; human. [Q8IXA5-1]
DR   CTD; 124912; -.
DR   DisGeNET; 124912; -.
DR   GeneCards; SPACA3; -.
DR   HGNC; HGNC:16260; SPACA3.
DR   HPA; ENSG00000141316; Tissue enriched (testis).
DR   MIM; 612749; gene.
DR   neXtProt; NX_Q8IXA5; -.
DR   OpenTargets; ENSG00000141316; -.
DR   PharmGKB; PA38101; -.
DR   VEuPathDB; HostDB:ENSG00000141316; -.
DR   eggNOG; ENOG502S1F5; Eukaryota.
DR   GeneTree; ENSGT00940000161810; -.
DR   HOGENOM; CLU_111620_1_1_1; -.
DR   InParanoid; Q8IXA5; -.
DR   OMA; MYCTDLL; -.
DR   PhylomeDB; Q8IXA5; -.
DR   TreeFam; TF324882; -.
DR   PathwayCommons; Q8IXA5; -.
DR   SignaLink; Q8IXA5; -.
DR   BioGRID-ORCS; 124912; 13 hits in 1067 CRISPR screens.
DR   ChiTaRS; SPACA3; human.
DR   GeneWiki; SPACA3; -.
DR   GenomeRNAi; 124912; -.
DR   Pharos; Q8IXA5; Tbio.
DR   PRO; PR:Q8IXA5; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q8IXA5; protein.
DR   Bgee; ENSG00000141316; Expressed in left testis and 104 other tissues.
DR   ExpressionAtlas; Q8IXA5; baseline and differential.
DR   Genevisible; Q8IXA5; HS.
DR   GO; GO:0043159; C:acrosomal matrix; IDA:UniProtKB.
DR   GO; GO:0002080; C:acrosomal membrane; IDA:UniProtKB.
DR   GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; IBA:GO_Central.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IMP:UniProtKB.
DR   GO; GO:0042117; P:monocyte activation; TAS:UniProtKB.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; TAS:UniProtKB.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; TAS:UniProtKB.
DR   GO; GO:0035036; P:sperm-egg recognition; IEA:Ensembl.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR030058; LYZL3.
DR   PANTHER; PTHR11407; PTHR11407; 1.
DR   PANTHER; PTHR11407:SF25; PTHR11407:SF25; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasmic vesicle; Direct protein sequencing;
KW   Disulfide bond; Membrane; Reference proteome; Secreted; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..215
FT                   /note="Sperm acrosome membrane-associated protein 3,
FT                   membrane form"
FT                   /id="PRO_0000256219"
FT   CHAIN           88..215
FT                   /note="Sperm acrosome membrane-associated protein 3,
FT                   processed form"
FT                   /id="PRO_0000256220"
FT   TOPO_DOM        1..63
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..215
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          88..215
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   SITE            87..88
FT                   /note="Cleavage; to produce processed form"
FT                   /evidence="ECO:0000305"
FT   DISULFID        93..213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        117..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        151..166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        162..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   VAR_SEQ         1..69
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_021329"
FT   VARIANT         80
FT                   /note="C -> Y (in dbSNP:rs16967845)"
FT                   /id="VAR_028885"
FT   VARIANT         100
FT                   /note="H -> R (in dbSNP:rs28963)"
FT                   /id="VAR_028886"
FT   VARIANT         128
FT                   /note="A -> T (in dbSNP:rs35420663)"
FT                   /id="VAR_050008"
SQ   SEQUENCE   215 AA;  23431 MW;  39988565D592BCC8 CRC64;
     MVSALRGAPL IRVHSSPVSS PSVSGPRRLV SCLSSQSSAL SQSGGGSTSA AGIEARSRAL
     RRRWCPAGIM LLALVCLLSC LLPSSEAKLY GRCELARVLH DFGLDGYRGY SLADWVCLAY
     FTSGFNAAAL DYEADGSTNN GIFQINSRRW CSNLTPNVPN VCRMYCSDLL NPNLKDTVIC
     AMKITQEPQG LGYWEAWRHH CQGKDLTEWV DGCDF
 
 
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