ID   FSCB_BOVIN              Reviewed;         818 AA.
AC   Q2T9N0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Fibrous sheath CABYR-binding protein;
GN   Name=FSCB {ECO:0000312|EMBL:AAI11348.1};
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] {ECO:0000312|EMBL:AAI11348.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI11348.1};
RC   TISSUE=Liver {ECO:0000312|EMBL:AAI11348.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the later stages of fibrous sheath
CC       biogenesis and spermatozoa capacitation. Inhibits ROPN1 and ROPN1L
CC       SUMOylation. Binds calcium. {ECO:0000250|UniProtKB:A1EGX6}.
CC   -!- SUBUNIT: Interacts with CABYR. Interacts with ROPN1 and ROPN1L; the
CC       interaction increases upon spermatozoa capacitation conditions.
CC       {ECO:0000250|UniProtKB:A1EGX6}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000250|UniProtKB:A1EGX6}. Note=Localizes to cortex of the fibrous
CC       sheath including the surface of the longitudinal columns and ribs of
CC       the principal piece of sperm flagella. {ECO:0000250|UniProtKB:A1EGX6}.
CC   -!- PTM: Phosphorylated by PKA upon spermatozoa capacitation conditions.
CC       {ECO:0000250|UniProtKB:A1EGX6}.
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DR   EMBL; BC111347; AAI11348.1; -; mRNA.
DR   RefSeq; NP_001070014.1; NM_001076546.2.
DR   AlphaFoldDB; Q2T9N0; -.
DR   IntAct; Q2T9N0; 1.
DR   MINT; Q2T9N0; -.
DR   STRING; 9913.ENSBTAP00000050184; -.
DR   PaxDb; Q2T9N0; -.
DR   PRIDE; Q2T9N0; -.
DR   GeneID; 767821; -.
DR   KEGG; bta:767821; -.
DR   CTD; 84075; -.
DR   eggNOG; ENOG502S90R; Eukaryota.
DR   InParanoid; Q2T9N0; -.
DR   OrthoDB; 341336at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
DR   InterPro; IPR043375; FSCB.
DR   PANTHER; PTHR36135; PTHR36135; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell projection; Cilium; Flagellum; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..818
FT                   /note="Fibrous sheath CABYR-binding protein"
FT                   /id="PRO_0000331224"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..305
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..460
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..508
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..797
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A1EGX6"
FT   MOD_RES         57
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A1EGX6"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A1EGX6"
SQ   SEQUENCE   818 AA;  87760 MW;  5E848FBFC4348C62 CRC64;
     MEEKDESEQS ISAGRQEIRK RRRPSQPMVD KSQQTEVTEK KKQLSIPQSS GPKAALSIGN
     IPGSKLNYEC HRVSSQLQQT WIKRKRVQDM ADKSLQTETI AEEKKEEIKL VCEAVVPEEK
     PAAVEVGPEF PESVREVEVP PNRYSVQVKI DRSQQTTCTG DWTMMNFPQK EKLDKEQQTY
     FSESEIVVIG WPTNSFSKSK EGAQKRKSSG NIFLSEHPEF QPTTSSNEEI RRPSISRTVS
     ISPTKKDSPV PLEDEKDVPV EVQPPAAEEI SAEEQLPLAE TTSEEVPVAV QPPPAEEPPL
     EAQPSPTEEA PGDEAPAKVE PTPAEEALSE KPPAEEALVE IQPSPVEEAA GDEAPAKVEA
     TSSEETLLKE PLTEVQPPAA EEAPIQDTPE LQLSPAVEAP AEEAPAEAEP PPAEEAPAEE
     APEVQSPPAE EAPAEEPPEI QSPPAEEAPA EEPPEVQSPP AEEAPAEEAP EVQSPPAEEA
     PAEEPPEVQS PPAEEVPAGE PPEVQSPPAE EAPAEEAPEV QSPPAEEVPA EEALAEVEPP
     PAEEAPAGEP SEVQSPPAEE APAEEAPEVQ SPPSEEAPAE EAPEVQSVPA GQAPAEEPLE
     VQPPPAEDAT EEEASEVQSL PTDEAPAEEG LGFQSPPADK APEEEAPEVQ SPPAEEAPAE
     EPPEVQSLPA DEAPAEEATE EVQSPPTEES PAEEAPAELQ PPSTEETTSE MVSVEKQPSL
     TEEPFITPIS LEETSAEVLL PPFEQTPADE ALVENVSPVD QAPKEADVLV EKLESGNLDD
     KPKSEEPLER DTIPKDSSGT KNEGVSFEIK GVIHIELE