S10AA_RAT
ID S10AA_RAT Reviewed; 95 AA.
AC P05943; Q5BJ98;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
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=Nerve growth factor-induced protein 42C;
DE AltName: Full=S100 calcium-binding protein A10;
DE AltName: Full=p10 protein;
DE AltName: Full=p11;
GN Name=S100a10;
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 [MRNA].
RX PubMed=3422491; DOI=10.1073/pnas.85.4.1277;
RA Masiakowski P., Shooter E.M.;
RT "Nerve growth factor induces the genes for two proteins related to a family
RT of calcium-binding proteins in PC12 cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1277-1281(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Park J.-Y., Kim W.-J., Chun S.-Y.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [4]
RP PROTEIN SEQUENCE OF 38-54, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [5]
RP INTERACTION WITH SCN10A.
RX PubMed=12050667; DOI=10.1038/nature00781;
RA Okuse K., Malik-Hall M., Baker M.D., Poon W.-Y.L., Kong H., Chao M.V.,
RA Wood J.N.;
RT "Annexin II light chain regulates sensory neuron-specific sodium channel
RT expression.";
RL Nature 417:653-656(2002).
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
CC (PubMed:12050667). Interacts with TASOR (By similarity).
CC {ECO:0000250|UniProtKB:P08207, ECO:0000250|UniProtKB:P60903,
CC ECO:0000269|PubMed:12050667}.
CC -!- INTERACTION:
CC P05943; Q62968: Scn10a; NbExp=4; IntAct=EBI-1800351, EBI-1800320;
CC -!- INDUCTION: By nerve growth factor.
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 EMBL; J03627; AAA42097.1; -; mRNA.
DR EMBL; AF465254; AAO33353.1; -; Genomic_DNA.
DR EMBL; BC091565; AAH91565.1; -; mRNA.
DR PIR; A31373; A31373.
DR RefSeq; NP_112376.1; NM_031114.1.
DR AlphaFoldDB; P05943; -.
DR SMR; P05943; -.
DR IntAct; P05943; 6.
DR STRING; 10116.ENSRNOP00000037097; -.
DR iPTMnet; P05943; -.
DR PhosphoSitePlus; P05943; -.
DR jPOST; P05943; -.
DR PaxDb; P05943; -.
DR PRIDE; P05943; -.
DR Ensembl; ENSRNOT00000120014; ENSRNOP00000096575; ENSRNOG00000023226.
DR GeneID; 81778; -.
DR KEGG; rno:81778; -.
DR UCSC; RGD:628655; rat.
DR CTD; 6281; -.
DR RGD; 628655; S100a10.
DR eggNOG; ENOG502S6TB; Eukaryota.
DR GeneTree; ENSGT00940000154197; -.
DR HOGENOM; CLU_138624_2_1_1; -.
DR InParanoid; P05943; -.
DR OMA; SEMEHAP; -.
DR OrthoDB; 1508691at2759; -.
DR PhylomeDB; P05943; -.
DR TreeFam; TF332727; -.
DR Reactome; R-RNO-75205; Dissolution of Fibrin Clot.
DR PRO; PR:P05943; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000023226; Expressed in duodenum and 20 other tissues.
DR ExpressionAtlas; P05943; baseline and differential.
DR Genevisible; P05943; RN.
DR GO; GO:1990665; C:AnxA2-p11 complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098797; C:plasma membrane protein complex; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
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:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0001765; P:membrane raft assembly; ISO:RGD.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051099; P:positive regulation of binding; ISO:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0045595; P:regulation of cell differentiation; NAS:RGD.
DR GO; GO:0001558; P:regulation of cell growth; NAS:RGD.
DR GO; GO:0050767; P:regulation of neurogenesis; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006900; P:vesicle budding from membrane; ISO:RGD.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Reference proteome.
FT CHAIN 1..95
FT /note="Protein S100-A10"
FT /id="PRO_0000144006"
FT DOMAIN 47..82
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 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"
SQ SEQUENCE 95 AA; 11075 MW; EC12960C177F1BBC CRC64;
MPSQMEHAME TMMLTFHRFA GEKNYLTKED LRVLMEREFP GFLENQKDPL AVDKIMKDLD
QCRDGKVGFQ SFLSLVAGLI IACNDYFVVH MKQKK
