ID   SPAT6_BOVIN             Reviewed;         487 AA.
AC   Q2KJG1;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Spermatogenesis-associated protein 6;
DE   Flags: Precursor;
GN   Name=SPATA6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for formation of the sperm connecting piece during
CC       spermiogenesis. Sperm connecting piece is essential for linking the
CC       developing flagellum to the head during late spermiogenesis. May be
CC       involved in myosin-based microfilament transport through interaction
CC       with myosin subunits. {ECO:0000250|UniProtKB:Q3U6K5}.
CC   -!- SUBUNIT: Interacts with MYL6. {ECO:0000250|UniProtKB:Q3U6K5}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3U6K5}. Cell
CC       projection, cilium, flagellum {ECO:0000250|UniProtKB:Q3U6K5}.
CC       Note=Specifically localizes to the segmented columns and the capitulum
CC       of the sperm connecting piece. {ECO:0000250|UniProtKB:Q3U6K5}.
CC   -!- SIMILARITY: Belongs to the SPATA6 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC105360; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC105360; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; Q2KJG1; -.
DR   STRING; 9913.ENSBTAP00000004068; -.
DR   PaxDb; Q2KJG1; -.
DR   PRIDE; Q2KJG1; -.
DR   eggNOG; ENOG502QRV3; Eukaryota.
DR   InParanoid; Q2KJG1; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0097224; C:sperm connecting piece; ISS:UniProtKB.
DR   GO; GO:0032027; F:myosin light chain binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0044458; P:motile cilium assembly; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   InterPro; IPR027207; Spata6.
DR   InterPro; IPR042769; SPATA6_fam.
DR   InterPro; IPR032732; SPATA6_N.
DR   PANTHER; PTHR16435; PTHR16435; 1.
DR   PANTHER; PTHR16435:SF3; PTHR16435:SF3; 1.
DR   Pfam; PF14909; SPATA6; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Developmental protein; Differentiation; Flagellum;
KW   Glycoprotein; Isopeptide bond; Phosphoprotein; Reference proteome;
KW   Secreted; Signal; Spermatogenesis; Ubl conjugation.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..487
FT                   /note="Spermatogenesis-associated protein 6"
FT                   /id="PRO_0000278440"
FT   REGION          170..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH7"
FT   MOD_RES         218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH7"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U6K5"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT   MOD_RES         486
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        247
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH7"
SQ   SEQUENCE   487 AA;  56137 MW;  2D403415120F62E1 CRC64;
     MPKVKALQCA LALEIRSVTC PGVVLKDKED IYLSICVFGQ YKKTQCVPAN FPLVFNARMV
     FEKVFPEAVD PGDVVAQLEY DTALFELIQL VPPVGETLST YDENTRDFMF PGPNQISGHH
     DSNRQVTMRR ISGLRGIAPK LEFSTTSVIT ECLISSRKCR TQDKFVYHTA PVEKPHSRLQ
     NRTSRSQKKK SKSPERNKYC INAKNYEQPT TSKSHSPSPY TKRRMCELSE DTRRRLAHLN
     LGPYEFKKET DKPPFVIRHV DPPSPRADAL FGSPGRDCER DGWSRLHNDH SHLGCYRPKD
     YKVIRTPHGR DFDESLERCE DYLSSRSCSK PQHSARTLLV HSAPSTMPKH SPSPVLNRAS
     LRERFHSDWC SPSNCDEIHD RVKNVLKSHQ AHQRHLYDER DPEKEDELEL KRGLLYRDSA
     YDSDPEYSSF QRPRGTLHLD DGEYWSNRAA SYKGKSHRPI FENSMDKIYR NLYKKACSSV
     SHTQESF