ID   MSP2_ASCSU              Reviewed;         127 AA.
AC   P27440;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Major sperm protein isoform beta;
DE   AltName: Full=Beta-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   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   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), AND SEQUENCE REVISION TO 114.
RX   PubMed=9501910; DOI=10.1038/nsb0398-184;
RA   Bullock T.L., McCoy A.J., Kent H.M., Roberts T.M., Stewart M.;
RT   "Structural basis for amoeboid motility in nematode sperm.";
RL   Nat. Struct. Biol. 5:184-189(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   -!- INTERACTION:
CC       P27440; P27440: -; NbExp=2; IntAct=EBI-15696003, EBI-15696003;
CC   -!- SUBCELLULAR LOCATION: Cell projection, pseudopodium. Cytoplasm,
CC       cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Sperm.
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DR   PDB; 2MSP; X-ray; 3.30 A; A/B/C/D/E/F/G/H=2-127.
DR   PDBsum; 2MSP; -.
DR   AlphaFoldDB; P27440; -.
DR   SMR; P27440; -.
DR   DIP; DIP-29889N; -.
DR   iPTMnet; P27440; -.
DR   EvolutionaryTrace; P27440; -.
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   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 beta"
FT                   /id="PRO_0000213434"
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. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..16
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   STRAND          42..49
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   STRAND          68..75
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   TURN            80..82
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   STRAND          89..96
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:2MSP"
FT   STRAND          112..126
FT                   /evidence="ECO:0007829|PDB:2MSP"
SQ   SEQUENCE   127 AA;  14248 MW;  718E4AFFDF787B33 CRC64;
     MAQSVPPGDI NTQPGSKIVF NAPYDDKHTY HIKITNAGGR RIGWAIKTTN MRRLGVDPPC
     GVLDPKESVL MAVSCDTFNA ATEDLNNDRI TIEWTNTPDG AAKQFRREWF QGDGMVRRKN
     LPIEYNL