S10AA_PIG
ID S10AA_PIG Reviewed; 96 AA.
AC P04163;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Protein S100-A10;
DE AltName: Full=Calpactin I light chain;
DE AltName: Full=Calpactin-1 light chain;
DE AltName: Full=Cellular ligand of annexin II;
DE AltName: Full=S100 calcium-binding protein A10;
DE AltName: Full=p10 protein;
DE AltName: Full=p11;
GN Name=S100A10;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE OF 2-96.
RC TISSUE=Intestinal epithelium;
RX PubMed=2998764; DOI=10.1002/j.1460-2075.1985.tb04023.x;
RA Gerke V., Weber K.;
RT "The regulatory chain in the p36-kd substrate complex of viral tyrosine-
RT specific protein kinases is related in sequence to the S-100 protein of
RT glial cells.";
RL EMBO J. 4:2917-2920(1985).
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}.
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DR PIR; A03079; LUPG10.
DR AlphaFoldDB; P04163; -.
DR SMR; P04163; -.
DR IntAct; P04163; 1.
DR STRING; 9823.ENSSSCP00000007051; -.
DR PaxDb; P04163; -.
DR PeptideAtlas; P04163; -.
DR PRIDE; P04163; -.
DR eggNOG; ENOG502S6TB; Eukaryota.
DR HOGENOM; CLU_138624_2_1_1; -.
DR InParanoid; P04163; -.
DR OMA; SEMEHAP; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P04163; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isopeptide bond;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2998764"
FT CHAIN 2..96
FT /note="Protein S100-A10"
FT /id="PRO_0000144005"
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 96 AA; 11075 MW; AE03A6E7DD7A8D65 CRC64;
MPSQMEHAME TMMFTFHKFA GDKGYLTKED LRVLMEKEFP GFLENQKDPL AVDKIMKDLD
QCRDGKVGFQ SFFSLIAGLT IACNDYFVVH MKQKGK
