FSCB_MOUSE
ID FSCB_MOUSE Reviewed; 1074 AA.
AC A1EGX6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Fibrous sheath CABYR-binding protein;
DE AltName: Full=PKA-phosphorylated calcium and CABYR-binding protein;
GN Name=Fscb {ECO:0000312|MGI:MGI:3646964};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABL63912.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1056-1063, FUNCTION,
RP INTERACTION WITH CABYR, CALCIUM-BINDING, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-25; SER-57;
RP SER-186; SER-275; SER-365 AND SER-1020, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:ABL63912.1};
RX PubMed=17855365; DOI=10.1074/jbc.m702238200;
RA Li Y.-F., He W., Jha K.N., Klotz K., Kim Y.-H., Mandal A., Pulido S.,
RA Digilio L., Flickinger C.J., Herr J.C.;
RT "FSCB, a novel protein kinase A-phosphorylated calcium-binding protein, is
RT a CABYR-binding partner involved in late steps of fibrous sheath
RT biogenesis.";
RL J. Biol. Chem. 282:34104-34119(2007).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP PHOSPHORYLATION BY PKA.
RX PubMed=21871179; DOI=10.5483/bmbrep.2011.44.8.541;
RA Liu S.L., Ni B., Wang X.W., Huo W.Q., Zhang J., Tian Z.Q., Huang Z.M.,
RA Tian Y., Tang J., Zheng Y.H., Jin F.S., Li Y.F.;
RT "FSCB phosphorylation in mouse spermatozoa capacitation.";
RL BMB Rep. 44:541-546(2011).
RN [4]
RP FUNCTION, PHOSPHORYLATION, INTERACTION WITH ROPN1 AND ROPN1L, AND TISSUE
RP SPECIFICITY.
RX PubMed=27398160;
RA Zhang X., Chen M., Yu R., Liu B., Tian Z., Liu S.;
RT "FSCB phosphorylation regulates mouse spermatozoa capacitation through
RT suppressing SUMOylation of ROPN1/ROPN1L.";
RL Am. J. Transl. Res. 8:2776-2782(2016).
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:0000269|PubMed:17855365,
CC ECO:0000269|PubMed:27398160}.
CC -!- SUBUNIT: Interacts with CABYR (PubMed:17855365). Interacts with ROPN1
CC and ROPN1L; the interaction increases upon spermatozoa capacitation
CC conditions (PubMed:27398160). {ECO:0000269|PubMed:17855365,
CC ECO:0000269|PubMed:27398160}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:17855365}. 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:0000269|PubMed:17855365}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to testis and epididymis,
CC expressed by spermatozoa. {ECO:0000269|PubMed:17855365,
CC ECO:0000269|PubMed:27398160}.
CC -!- DEVELOPMENTAL STAGE: First expressed at step 11 of spermatogenesis in
CC the elongating spermatids, and subsequently incorporates into the
CC flagellar principal piece of the sperm. {ECO:0000269|PubMed:17855365}.
CC -!- PTM: Phosphorylated by PKA upon spermatozoa capacitation conditions.
CC {ECO:0000269|PubMed:17855365, ECO:0000269|PubMed:21871179,
CC ECO:0000269|PubMed:27398160}.
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DR EMBL; EF133693; ABL63912.1; -; mRNA.
DR AlphaFoldDB; A1EGX6; -.
DR STRING; 10090.ENSMUSP00000051554; -.
DR iPTMnet; A1EGX6; -.
DR PRIDE; A1EGX6; -.
DR ProteomicsDB; 271608; -.
DR MGI; MGI:3646964; Fscb.
DR eggNOG; ENOG502S90R; Eukaryota.
DR InParanoid; A1EGX6; -.
DR ChiTaRS; Fscb; mouse.
DR PRO; PR:A1EGX6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A1EGX6; protein.
DR GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI.
DR GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:UniProtKB.
DR InterPro; IPR043375; FSCB.
DR PANTHER; PTHR36135; PTHR36135; 2.
PE 1: Evidence at protein level;
KW Calcium; Cell projection; Cilium; Direct protein sequencing; Flagellum;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1074
FT /note="Fibrous sheath CABYR-binding protein"
FT /id="PRO_0000331225"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..561
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..623
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17855365"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17855365"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17855365"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17855365"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17855365"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17855365"
SQ SEQUENCE 1074 AA; 114979 MW; F45159A44CB8BCDD CRC64;
MEECEEPEEP ISLGRQEYRR RRRPSQPMVD KSQQTEITEK RKAMASVQPP APKATHSIGN
IPGSKDNYSR KEYESLRLSS QLQKTLMKRK HVQDMTDKSL QTEPIVEEKV EVIFIDKTLK
LEENTAGVGE IAPELPQSIP EVEIPTSRPT SHLIDRSQQT SCTGDWSLIY ICPKEKVDKE
QQTYFSELEI IIRSIPGSSM TKSKEETIPI AQEDPLVEIN GSLEIEVLSP EELPDVMMSF
TEGEISGELQ ALSNGEATVK GELFLTEEIP IQAPSPAEET SAAETATTTA KDVVDIQAPP
ADKLSSVEAP ADISPTLVQG ALSDKPSDQQ YPQGTEMAPS ELPVEDLDPF SEEVLEKVQA
LTTDSMLEDL GIAESTIAEE TSGKVQHPLS EETSKEVPAE VHFPIAADFE ESAILINEKF
ATDEVFEEYK PPIIEEVSAD KATAEVQPPS AEDASEEVAS SEVLPPSTEQ GTVEDLTAEV
LSTPTEEGPT EVPPQPTEEG PAEVPPPLSE EGPAEVPPAP AEEAPAEVLP PPAEEAPAEV
PPPLTEEGPA EVPPPLTEEG PAEVPLAPAE EVPAEFLPPP AEEVPAEVPP PLTEEGPAEV
PPPLTEEGPE EVPPLPAEEA PTKVPPSPAE KGSAEVSPPQ TEEGPAEVPP PPAEEFPTEV
PSSSAEEGSS EVPLPPTAER PEEAPPPATE EAPVEVLPPA TEEAPVEVLP PATEEAPVEV
QSPAAEEGLA EVPPPPTEES PTHDVPTEVQ VPQAKESPGQ VLPLSGESTA EEASAQVQPP
SFEKAPLESL PLEEVEKIHL DNLPFEVQPL PTEDIAIGVP AESQALPADE NPAREDTVET
QPSSFEGAPI AENPIEAPLP ASEADTGRED SAVHPSSLGP TDEAPAEIQI LQTDDIPTEM
SPVENQPLPA EEGFPEVVSE EEATAAEVRF PLSEGAPAQE ATVEAQLTSV EESPKRASVD
VQPLSPETPV EESPGVDLPL KTNEVTMQEF RVEKMPAEDS LPPSEQTPAD QVLLKEHRLS
QVADISEKEL ESTTLTSDKM SEGIDSVPED VSGTKDDQIS TFKIEGTIKI ELKN
