ID SP17_MONDO Reviewed; 179 AA.
AC O62771;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Sperm surface protein Sp17;
DE AltName: Full=Sperm autoantigenic protein 17;
GN Name=SPA17; Synonyms=SP17;
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Wen Y., O'Rand M.G.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sperm surface zona pellucida binding protein. Helps to bind
CC spermatozoa to the zona pellucida with high affinity. Might function in
CC binding zona pellucida and carbohydrates (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. May interact with ROPN1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis- and sperm-specific.
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DR EMBL; AF054290; AAC08025.1; -; mRNA.
DR RefSeq; NP_001028164.1; NM_001032992.1.
DR AlphaFoldDB; O62771; -.
DR SMR; O62771; -.
DR STRING; 13616.ENSMODP00000004559; -.
DR GeneID; 554229; -.
DR KEGG; mdo:554229; -.
DR CTD; 53340; -.
DR eggNOG; ENOG502S4R6; Eukaryota.
DR HOGENOM; CLU_115900_0_0_1; -.
DR InParanoid; O62771; -.
DR OrthoDB; 5472182at2759; -.
DR Proteomes; UP000002280; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035686; C:sperm fibrous sheath; IBA:GO_Central.
DR GO; GO:0097228; C:sperm principal piece; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:InterPro.
DR CDD; cd12100; DD_CABYR_SP17; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR047579; DD_CABYR_SP17.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR012105; Sp17.
DR PANTHER; PTHR10699; NEUROMODULIN; 1.
DR PANTHER; PTHR10699:SF11; ZGC:153721; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF016533; Sp17; 1.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR PROSITE; PS50096; IQ; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome.
FT CHAIN 1..179
FT /note="Sperm surface protein Sp17"
FT /id="PRO_0000181343"
FT DOMAIN 143..172
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 72..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..136
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 179 AA; 20864 MW; CADDC13CEC66A00E CRC64;
MSIPFSNTHY RIPQGFGNLL EGLTREILRE QPDNIPAFAA AYFENLLEKR EKTNFDPAEW
GAKVDDRFYN NHAFKDEPPE KSETQKIQPE KVAIEKETMP QETVKEKETQ VSFVEEPTEE
PQKEEEEEED EEDLEGLLVR EGMQDAAVKI QAVFRGHKTR KEYLKKRDST DETADENNE
//
