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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
 
 
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