CABS1_RAT
ID CABS1_RAT Reviewed; 390 AA.
AC Q68FX6; Q9JI16;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Calcium-binding and spermatid-specific protein 1;
DE AltName: Full=Casein-like phosphoprotein;
DE AltName: Full=Protein RSD-6;
GN Name=Cabs1; Synonyms=Clph, Rsd6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 9-15; 235-245; 250-270 AND 271-294, IDENTIFICATION BY
RP MASS SPECTROMETRY, PHOSPHORYLATION AT THR-280, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND CALCIUM-BINDING.
RX PubMed=19271754; DOI=10.1021/pr900082m;
RA Calvel P., Kervarrec C., Lavigne R., Vallet-Erdtmann V., Guerrois M.,
RA Rolland A., Chalmel F., Jegou B., Pineau C.;
RT "CLPH, a novel casein kinase 2-phosphorylated disordered protein, is
RT specificallya associated with post-meiotic germ cells in rat
RT spermatogenesis.";
RL J. Proteome Res. 8:2953-2965(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-390.
RC TISSUE=Testis;
RA Wang L., Miao S., Gou D., Zhang X., Ying H., Yang J., Ma H.;
RT "A new gene from rat testis cDNA library.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-267; THR-280;
RP SER-312; SER-346; SER-356; SER-371 AND SER-375, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Calcium-binding protein (PubMed:19271754). Essential for
CC maintaining the structural integrity of the sperm flagella (By
CC similarity). {ECO:0000250|UniProtKB:Q8C633,
CC ECO:0000269|PubMed:19271754}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19271754}.
CC Mitochondrion inner membrane {ECO:0000269|PubMed:19271754}. 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 (PubMed:19271754). Localizes to the principal
CC piece of the sperm flagellum (By similarity).
CC {ECO:0000250|UniProtKB:Q8C633, ECO:0000269|PubMed:19271754}.
CC -!- TISSUE SPECIFICITY: Expressed in seminiferous tubules of the testis in
CC step 10 spermatids (stage X), subsequently increasing to reach maximal
CC levels of step 18 elongated spermatids (stage VI) (at protein level).
CC Strongly expressed in testis. Weakly expressed in olfactory epithelium.
CC Expressed in spermatids of seminiferous tubules at steps 4-14 (stages
CC IV to XIV of the seminiferous epithelium classification).
CC {ECO:0000269|PubMed:19271754}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76188.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC079062; AAH79062.1; -; mRNA.
DR EMBL; AF271155; AAF76188.1; ALT_INIT; mRNA.
DR RefSeq; NP_071599.2; NM_022263.2.
DR AlphaFoldDB; Q68FX6; -.
DR STRING; 10116.ENSRNOP00000002670; -.
DR iPTMnet; Q68FX6; -.
DR PhosphoSitePlus; Q68FX6; -.
DR PaxDb; Q68FX6; -.
DR PRIDE; Q68FX6; -.
DR Ensembl; ENSRNOT00000002670; ENSRNOP00000002670; ENSRNOG00000001950.
DR GeneID; 64029; -.
DR KEGG; rno:64029; -.
DR UCSC; RGD:620592; rat.
DR CTD; 85438; -.
DR RGD; 620592; Cabs1.
DR eggNOG; ENOG502RWWC; Eukaryota.
DR GeneTree; ENSGT00390000015647; -.
DR HOGENOM; CLU_719537_0_0_1; -.
DR InParanoid; Q68FX6; -.
DR OMA; KITEPFS; -.
DR OrthoDB; 1176309at2759; -.
DR PhylomeDB; Q68FX6; -.
DR TreeFam; TF338174; -.
DR PRO; PR:Q68FX6; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000001950; Expressed in testis and 4 other tissues.
DR Genevisible; Q68FX6; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
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; IEP:RGD.
DR InterPro; IPR026118; Ca-bd_spermatid.
DR PANTHER; PTHR22810; PTHR22810; 2.
DR Pfam; PF15367; CABS1; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Flagellum; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..390
FT /note="Calcium-binding and spermatid-specific protein 1"
FT /id="PRO_0000339181"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 280
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:19271754,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 390 AA; 42256 MW; F055BE52443A377B CRC64;
MAEDGSPKIY SRPPRDSSKT PTEADIFFGA DNTIPKSETT ITSEGDHITS VNDCTADGDF
STTVNKLTPT KEKLKLEEDI EASLKSTTLP EKEITTPTET TNSKPKESIT ENFIPVKIGN
ISSPVGTVSL IDFSSNMAKE DILLATIDAE DKEVKPTTEL SETQEDSSAN DEDTSVPPDE
NTETDVSSST SSDVPDDGAV QVTDSFSPES DVPPSTEKEV TTIPDNVAED KVTKIDLIVS
EDRPKTVTKL SDSEEEKFIT VFELTNSAEK AKDNPEDPLT DEEPADGVNT WVEKDAANEA
ESHAVLLTAV ESRYDFVVTA SETNSVVVEE PHVDTKNSPE KDAAESVTNV TEEFPSVTSV
VEQSGNKEDL STNDSGIFKL LKEEPDELMM
