CABYR_MACFA
ID CABYR_MACFA Reviewed; 487 AA.
AC Q4R3X7; Q4R394; Q4R3Y9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Calcium-binding tyrosine phosphorylation-regulated protein;
GN Name=CABYR; ORFNames=QtsA-13213, QtsA-13395, QtsA-18586;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as a regulator of both motility- and head-
CC associated functions such as capacitation and the acrosome reaction.
CC May bind calcium in vitro (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FSCB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250}.
CC Note=Localized to fibrous sheath including the surface of the
CC longitudinal columns and ribs of the principal piece of sperm flagella.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues during in vitro capacitation.
CC Dephosphorylation affects its ability to bind calcium (By similarity).
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE02177.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE02189.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE02423.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB179126; BAE02177.1; ALT_INIT; mRNA.
DR EMBL; AB179138; BAE02189.1; ALT_FRAME; mRNA.
DR EMBL; AB179372; BAE02423.1; ALT_INIT; mRNA.
DR RefSeq; NP_001270695.1; NM_001283766.1.
DR RefSeq; XP_015295275.1; XM_015439789.1.
DR RefSeq; XP_015295276.1; XM_015439790.1.
DR RefSeq; XP_015295277.1; XM_015439791.1.
DR RefSeq; XP_015295278.1; XM_015439792.1.
DR AlphaFoldDB; Q4R3X7; -.
DR SMR; Q4R3X7; -.
DR STRING; 9541.XP_005587070.1; -.
DR Ensembl; ENSMFAT00000041134; ENSMFAP00000010521; ENSMFAG00000007440.
DR GeneID; 101926492; -.
DR KEGG; mcf:101926492; -.
DR CTD; 26256; -.
DR VEuPathDB; HostDB:ENSMFAG00000007440; -.
DR eggNOG; ENOG502S1NF; Eukaryota.
DR GeneTree; ENSGT00390000000444; -.
DR OMA; VHISSIY; -.
DR OrthoDB; 919811at2759; -.
DR Proteomes; UP000233100; Chromosome 18.
DR Bgee; ENSMFAG00000007440; Expressed in liver and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0097229; C:sperm end piece; IEA:Ensembl.
DR GO; GO:0035686; C:sperm fibrous sheath; IEA:Ensembl.
DR GO; GO:0097228; C:sperm principal piece; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0048240; P:sperm capacitation; IEA:InterPro.
DR InterPro; IPR038848; CABYR.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR PANTHER; PTHR15494; PTHR15494; 2.
DR Pfam; PF02197; RIIa; 1.
DR SMART; SM00394; RIIa; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..487
FT /note="Calcium-binding tyrosine phosphorylation-regulated
FT protein"
FT /id="PRO_0000089269"
FT DOMAIN 12..49
FT /note="RIIa"
FT REGION 78..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 231
FT /note="L -> P (in Ref. 1; BAE02189)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="M -> V (in Ref. 1; BAE02189)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="P -> L (in Ref. 1; BAE02177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 51866 MW; F80CED1744A9EAA4 CRC64;
MISSKPRLVV PYGLKTLLEG ISRAVLKTNP SDINQFAAAY FQELTMYRGN TTVDIKDLVK
QFHQIKVEKW SEGTTPQKKL ECLKEPEKTS VESKVPTQME KSTDTDEDNV TRTEYSDKTT
QFPSVYAEPG AEQTEAVGDS SSKPATPKAT TPPSSPPPTA VSPEFAYVPA DPAQLAAQML
GKVSSIHSDQ SDVLMVDVAT SMPVVIEEVP SSEAAEDVMV AAPLVCSGKV LEVQVVSQTS
VHVDLGSQPK ENEAEQSTAS SVPLQDEQEP PAYDQAPEVT LQADIEVMST VHISSVYNDV
PVIEGVVYIE QLPEQIVTPF TDQVACLKEN EQSPPVSPKS VVEKTTSGIS KKSVESVELA
QLEENAKYSS VYVEAEAAAL LSDTSLKGQP EVPAQLLDAE GAVKIGSEKS LHLEVGITSI
VSDNTGQEES GENSVPQEME GKPVLSGEAA EAVHSGTSVK SSSGPFPPAP EGLTAPEIEP
EGEATAE
