ID A0A0V0V300_9BILA Unreviewed; 288 AA.
AC A0A0V0V300;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Major sperm protein {ECO:0000256|RuleBase:RU003425};
DE Flags: Fragment;
GN ORFNames=T09_11348 {ECO:0000313|EMBL:KRX57828.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX57828.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX57828.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX57828.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Central component in molecular interactions underlying sperm
CC crawling. Forms an extensive filament system that extends from sperm
CC villipoda, along the leading edge of the pseudopod.
CC {ECO:0000256|RuleBase:RU003425}.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC family. {ECO:0000256|ARBA:ARBA00008932}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX57828.1}.
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DR EMBL; JYDN01000095; KRX57828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V300; -.
DR STRING; 181606.A0A0V0V300; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like_sf.
DR InterPro; IPR016763; VAP.
DR PANTHER; PTHR10809:SF144; MAJOR SPERM PROTEIN; 1.
DR PANTHER; PTHR10809; VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN; 1.
DR Pfam; PF00635; Motile_Sperm; 1.
DR SUPFAM; SSF49354; PapD-like; 1.
DR PROSITE; PS50202; MSP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU003425};
KW Cytoskeleton {ECO:0000256|RuleBase:RU003425};
KW Kinase {ECO:0000313|EMBL:KRX57828.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000313|EMBL:KRX57828.1}.
FT DOMAIN 30..147
FT /note="MSP"
FT /evidence="ECO:0000259|PROSITE:PS50202"
FT REGION 159..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX57828.1"
SQ SEQUENCE 288 AA; 31704 MW; C67A60B9C0BDF7F4 CRC64;
LFCYRIFYRC VRKPFEMEFN SSFLVSAARQ IFVEPQGMLV FKGPFNEAKN IDVKVTNMSQ
FRVAFKFRTT RPDGIKFRPP MGILSPGGEK YIKVRCLAIS GAPPAKDRCT LHCVALPPDY
RCVKPQDFWK SPDSKNVTTE RYPMKVIYEG VVPPTTEAET PAIPVEVKPA EEAKPVEEAK
PAEEAKPVEE AKPVEEAKPV EQAKPAEEAK PAEEAKPVEE AKPAEEAKSA EGAAAEEGEE
GKVVEEAAAP KSAEEASPVE GGEDKAGAKE GEEEEEEGDE EEEEEKGE
//
