CABS1_MACFA
ID CABS1_MACFA Reviewed; 396 AA.
AC Q95JW6; Q95JX2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Calcium-binding and spermatid-specific protein 1;
GN Name=CABS1; ORFNames=QtsA-12769, QtsA-13567;
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;
RA Hashimoto K., Osada N., Hida M., Kusuda J., Tanuma R., Hirai M., Terao K.,
RA Sugano S.;
RT "Isolation of novel full-length cDNA clones from macaque testis cDNA
RT libraries.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
CC -!- FUNCTION: Calcium-binding protein (By similarity). Essential for
CC maintaining the structural integrity of the sperm flagella (By
CC similarity). {ECO:0000250|UniProtKB:Q68FX6,
CC ECO:0000250|UniProtKB:Q8C633}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68FX6}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q68FX6}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8C633}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250|UniProtKB:Q8C633}. Note=Mostly cytoplasmic, but associated
CC with the mitochondrial inner membrane during the last steps of
CC spermatid differentiation. Localizes to the principal piece of the
CC sperm flagellum (By similarity). {ECO:0000250|UniProtKB:Q68FX6,
CC ECO:0000250|UniProtKB:Q8C633}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB070062; BAB63007.1; -; mRNA.
DR EMBL; AB070055; BAB63000.1; -; mRNA.
DR RefSeq; NP_001306306.1; NM_001319377.1.
DR AlphaFoldDB; Q95JW6; -.
DR SMR; Q95JW6; -.
DR STRING; 9541.XP_005555198.1; -.
DR GeneID; 102115510; -.
DR CTD; 85438; -.
DR eggNOG; ENOG502RWWC; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:InterPro.
DR InterPro; IPR026118; Ca-bd_spermatid.
DR PANTHER; PTHR22810; PTHR22810; 3.
DR Pfam; PF15367; CABS1; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle;
KW Flagellum; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..396
FT /note="Calcium-binding and spermatid-specific protein 1"
FT /id="PRO_0000339179"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FX6"
FT MOD_RES 288
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q68FX6"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FX6"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FX6"
FT CONFLICT 64
FT /note="A -> T (in Ref. 2; BAB63000)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="G -> S (in Ref. 2; BAB63000)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="T -> I (in Ref. 2; BAB63000)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="M -> I (in Ref. 2; BAB63000)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="S -> G (in Ref. 2; BAB63000)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="M -> I (in Ref. 2; BAB63000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 43214 MW; 4F5C048C1A56DA96 CRC64;
MAEDGLPKIY SHPPTESSKT PTAATIFFGA DNAIPKSETT ITSEGDHVTS VNEYVLESDF
STTADNKLTP TKEKLRSEDD MGTDFIKSTT HLQKEITSLT GTANSITRDS ITENFMTVKI
GNISSPVTTV SLIDFSTDIA KEDILLDTID TGDAEILITS EVSGTLKDSS AGVADTPAFP
RIKDEADMNN YNSSIKSNVP ADEAIQVTDS IIPEAEIPPA PEVNFTTIPD ITALEEEKMT
KIDLSVLEDD TSAVATLTDS DEEKFITVFE LTTSAEKDKD NQEDTLLTDE ESPEGANMWM
ERETATEAET HSVLLTAVES RYDFVVPASI ATNLVEDSST EEELSETDRT ETVPKITEPF
SGTSSVLDTP DYKEDTSTTE TDIFELLKEE PDEFMI