ID   MSP1_ASCSU              Reviewed;         127 AA.
AC   P27439; P27441;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Major sperm protein isoform alpha;
DE   AltName: Full=Alpha-MSP;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3770294; DOI=10.1016/0012-1606(86)90081-3;
RA   Bennett K.L., Ward S.;
RT   "Neither a germ line-specific nor several somatically expressed genes are
RT   lost or rearranged during embryonic chromatin diminution in the nematode
RT   Ascaris lumbricoides var. suum.";
RL   Dev. Biol. 118:141-147(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bullock T.L., Parathasathy G., King K.L., Kent M.L., Roberts T.M.,
RA   Stewart M.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-127, AND ACETYLATION AT ALA-2.
RC   TISSUE=Sperm;
RX   PubMed=1527183; DOI=10.1242/jcs.101.4.847;
RA   King K.L., Stewart M., Roberts T.M., Seavy M.;
RT   "Structure and macromolecular assembly of two isoforms of the major sperm
RT   protein (MSP) from the amoeboid sperm of the nematode, Ascaris suum.";
RL   J. Cell Sci. 101:847-857(1992).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=8913307; DOI=10.1006/jmbi.1996.0575;
RA   Bullock T.L., Roberts T.M., Stewart M.;
RT   "2.5-A resolution crystal structure of the motile major sperm protein (MSP)
RT   of Ascaris suum.";
RL   J. Mol. Biol. 263:284-296(1996).
RN   [5]
RP   STRUCTURE BY NMR.
RX   PubMed=9878374; DOI=10.1006/jmbi.1998.2291;
RA   Haaf A., Leclaire L. III, Roberts G., Kent H.M., Roberts T.M., Stewart M.,
RA   Neuhaus D.;
RT   "Solution structure of the motile major sperm protein (MSP) of Ascaris suum
RT   -- evidence for two manganese binding sites and the possible role of
RT   divalent cations in filament formation.";
RL   J. Mol. Biol. 284:1611-1624(1998).
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   -!- SUBUNIT: Forms filaments 10 nm wide, with a characteristic substructure
CC       repeating axially at 9 nm.
CC   -!- SUBCELLULAR LOCATION: Cell projection, pseudopodium. Cytoplasm,
CC       cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Sperm.
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DR   EMBL; M15680; AAA29375.1; -; Genomic_DNA.
DR   EMBL; X94249; CAA63933.1; -; mRNA.
DR   PIR; A45944; A45944.
DR   PDB; 1MSP; X-ray; 2.50 A; A/B=2-127.
DR   PDB; 2BVU; X-ray; 2.50 A; A/B/C/D=2-127.
DR   PDB; 3MSP; NMR; -; A/B=2-127.
DR   PDBsum; 1MSP; -.
DR   PDBsum; 2BVU; -.
DR   PDBsum; 3MSP; -.
DR   AlphaFoldDB; P27439; -.
DR   BMRB; P27439; -.
DR   SMR; P27439; -.
DR   iPTMnet; P27439; -.
DR   EnsemblMetazoa; AgB02_g504_t01; AgB02_g504_t01; AgB02_g504.
DR   EvolutionaryTrace; P27439; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000535; MSP_dom.
DR   InterPro; IPR008962; PapD-like_sf.
DR   Pfam; PF00635; Motile_Sperm; 1.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   PROSITE; PS50202; MSP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell projection; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1527183"
FT   CHAIN           2..127
FT                   /note="Major sperm protein isoform alpha"
FT                   /id="PRO_0000213433"
FT   DOMAIN          9..126
FT                   /note="MSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:1527183"
FT   CONFLICT        114
FT                   /note="G -> D (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..16
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          42..49
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          68..75
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          89..96
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:1MSP"
FT   STRAND          117..126
FT                   /evidence="ECO:0007829|PDB:1MSP"
SQ   SEQUENCE   127 AA;  14390 MW;  218DCEF6923FF67F CRC64;
     MAQSVPPGDI NTQPSQKIVF NAPYDDKHTY HIKITNAGGR RIGWAIKTTN MRRLSVDPPC
     GVLDPKEKVL MAVSCDTFNA ATEDLNNDRI TIEWTNTPDG AAKQFRREWF QGDGMVRRKN
     LPIEYNL