S10AA_RABIT
ID S10AA_RABIT Reviewed; 97 AA.
AC Q6SQH4;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein S100-A10;
DE AltName: Full=Calpactin I light chain;
DE AltName: Full=Calpactin-1 light chain;
DE AltName: Full=S100 calcium-binding protein A10;
DE AltName: Full=p10 protein;
GN Name=S100a10;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Wiehler W.B., Pho M.V.C., Walsh M.P.;
RT "Rabbit S100 calcium binding protein A10 mRNA.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Because S100A10 induces the dimerization of ANXA2/p36, it may
CC function as a regulator of protein phosphorylation in that the ANXA2
CC monomer is the preferred target (in vitro) of tyrosine-specific kinase.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2
CC heavy chains of ANXA2/p36 (By similarity). Interacts with SCN10A (By
CC similarity). Interacts with TASOR (By similarity).
CC {ECO:0000250|UniProtKB:P05943, ECO:0000250|UniProtKB:P08207,
CC ECO:0000250|UniProtKB:P60903}.
CC -!- MISCELLANEOUS: Does not appear to bind calcium. Contains 2 ancestral
CC calcium site related to EF-hand domains that have lost their ability to
CC bind calcium.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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; AY452731; AAR17457.1; -; mRNA.
DR RefSeq; NP_001075632.1; NM_001082163.1.
DR AlphaFoldDB; Q6SQH4; -.
DR SMR; Q6SQH4; -.
DR CORUM; Q6SQH4; -.
DR STRING; 9986.ENSOCUP00000004503; -.
DR Ensembl; ENSOCUT00000005196; ENSOCUP00000004503; ENSOCUG00000005198.
DR GeneID; 100008922; -.
DR KEGG; ocu:100008922; -.
DR CTD; 6281; -.
DR eggNOG; ENOG502S6TB; Eukaryota.
DR GeneTree; ENSGT00940000154197; -.
DR HOGENOM; CLU_138624_2_1_1; -.
DR InParanoid; Q6SQH4; -.
DR OMA; SEMEHAP; -.
DR OrthoDB; 1508691at2759; -.
DR TreeFam; TF332727; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000005198; Expressed in lung and 16 other tissues.
DR ExpressionAtlas; Q6SQH4; baseline.
DR CDD; cd05024; S-100A10; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR028476; S100-A10.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF74; PTHR11639:SF74; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 3: Inferred from homology;
KW Acetylation; Isopeptide bond; Reference proteome; Ubl conjugation.
FT CHAIN 1..97
FT /note="Protein S100-A10"
FT /id="PRO_0000236022"
FT REGION 60..71
FT /note="Ancestral calcium site"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60903"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P60903"
SQ SEQUENCE 97 AA; 11203 MW; 3E8E03A6E7DD7A8D CRC64;
MPSQMEHAME TMMFTFHKFA GDKGYLTKED LRVLMEKEFP GFLENQKDPL AVDKIMKDLD
QCRDGKVGFQ SFFSLIAGLT IACNDYFVVH MKQKGKK
