CABYR_VULVU
ID CABYR_VULVU Reviewed; 498 AA.
AC Q710D7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Calcium-binding tyrosine phosphorylation-regulated protein;
DE AltName: Full=Sperm protein 13;
DE AltName: Full=fSP13 autoantigen;
GN Name=CABYR; Synonyms=SP13;
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 270-283, SUBCELLULAR
RP LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15509732; DOI=10.1095/biolreprod.104.032623;
RA Verdier Y., Farre G., Rouet N., Kele Z., Janaky T., Boue F.;
RT "Identification of a new, testis-specific sperm antigen localized on the
RT principal piece of the spermatozoa tail in the fox (Vulpes vulpes).";
RL Biol. Reprod. 72:502-508(2005).
RN [2]
RP IDENTIFICATION BY 2D-PAGE.
RX PubMed=12065460;
RA Verdier Y., Rouet N., Artois M., Boue F.;
RT "Partial characterization of antigenic sperm proteins in foxes (Vulpes
RT vulpes).";
RL J. Androl. 23:529-536(2002).
CC -!- FUNCTION: May function as a regulator of both motility- and head-
CC associated functions such as capacitation and the acrosome reaction.
CC Binds calcium in vitro (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FSCB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15509732}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15509732}. Cell projection,
CC cilium, flagellum {ECO:0000269|PubMed:15509732}. Note=Localizes to
CC fibrous sheath of the principal piece of sperm flagella.
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:15509732}.
CC -!- PTM: Phosphorylated on tyrosine residues during in vitro capacitation.
CC Dephosphorylation affects its ability to bind calcium (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 4.3
CC to 4.6, its MW is: 97 kDa.
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DR EMBL; AJ421969; CAD19163.1; -; mRNA.
DR AlphaFoldDB; Q710D7; -.
DR SMR; Q710D7; -.
DR STRING; 9627.ENSVVUP00000003098; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 1: Evidence at protein level;
KW Calcium; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Flagellum; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..498
FT /note="Calcium-binding tyrosine phosphorylation-regulated
FT protein"
FT /id="PRO_0000089271"
FT DOMAIN 12..49
FT /note="RIIa"
FT REGION 74..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 53087 MW; CFD605645421BA32 CRC64;
MISSKPRLVV PYGLKTLLEG VSRAILKINP PNITQFAAVY FKELIVFREG NTSLDIKDLV
KQFHQIKVEK WSEGTTQEKE PECMEEQVET SVVSQEPTRM EKSTDTEEDN IAGPLFMNKT
TQFPSVHAEV LLEPEETPEA ACGGSPKPST PKAVTPPSSP SPAAVSQEFA YVPADPAQFA
AQMLGNVSSI HSDQSDVLMV DVATSMPVFS EEVLSSEAAE DARVAIPSVY SAEVVALQVL
SQTSVHVDLG PKPKDDEAEP TTASSFPLQD EQDPPAYDQA PEVPLQADIE VTSFVHVSSI
YNNEPVIEGV TYVEQIPEHI VIPFTDHVAS LKDNEPPDSP IPVACDTGMS EKTVGSVSLA
QLEVESHYSS VHMEAEASVL FSDTSLKGQP AQFPDAGGST KAVGSEKPLH LEVEFTALVP
GNSGQEESQG SSAAQEMEVK LVLSGEAATA VLSAASVRAA GGSPTPVPEG LTEPELEPEL
EAALEQGLMK PDAETTTV