HATA_DICDI
ID HATA_DICDI Reviewed; 118 AA.
AC P13231; Q54SW7;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Hisactophilin-1;
DE AltName: Full=Histidine-rich actin-binding protein 1;
DE Short=HS I;
GN Name=hatA; Synonyms=abpH; ORFNames=DDB_G0282141;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2914932; DOI=10.1016/s0021-9258(19)81688-5;
RA Scheel J., Ziegelbauer K., Kupke T., Humbel B.M., Noegel A.A., Gerisch G.,
RA Schleicher M.;
RT "Hisactophilin, a histidine-rich actin-binding protein from Dictyostelium
RT discoideum.";
RL J. Biol. Chem. 264:2832-2839(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION, AND MYRISTOYLATION AT GLY-2.
RC STRAIN=AX2, and AX3;
RX PubMed=7822284; DOI=10.1074/jbc.270.2.596;
RA Hanakam F., Eckerskorn C., Lottspeich F., Mueller-Taubenberger A.,
RA Schaefer W., Gerisch G.;
RT "The pH-sensitive actin-binding protein hisactophilin of Dictyostelium
RT exists in two isoforms which both are myristoylated and distributed between
RT plasma membrane and cytoplasm.";
RL J. Biol. Chem. 270:596-602(1995).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=1436061; DOI=10.1038/359855a0;
RA Habazetti J., Gondol D., Wiltschek R., Otlewski J., Schleicher M.,
RA Holak T.A.;
RT "Structure of hisactophilin is similar to interleukin-1 beta and fibroblast
RT growth factor.";
RL Nature 359:855-858(1992).
CC -!- FUNCTION: May act as an intracellular pH sensor that links chemotactic
CC signals to responses in the microfilament system of the cells by
CC nucleating actin polymerization or stabilizing the filaments.
CC -!- SUBUNIT: Homodimer or heterodimer of hatA and hatB, linked by a
CC disulfide bond.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Lipid-anchor;
CC Cytoplasmic side.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:7822284}.
CC -!- SIMILARITY: Belongs to the hisactophilin family. {ECO:0000305}.
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DR EMBL; J04472; AAA33218.1; -; mRNA.
DR EMBL; AAFI02000045; EAL66350.1; -; Genomic_DNA.
DR PIR; A31429; A31429.
DR RefSeq; XP_640342.1; XM_635250.1.
DR PDB; 1HCD; NMR; -; A=1-118.
DR PDB; 1HCE; NMR; -; A=1-118.
DR PDBsum; 1HCD; -.
DR PDBsum; 1HCE; -.
DR AlphaFoldDB; P13231; -.
DR SMR; P13231; -.
DR STRING; 44689.DDB0215335; -.
DR iPTMnet; P13231; -.
DR PaxDb; P13231; -.
DR EnsemblProtists; EAL66350; EAL66350; DDB_G0282141.
DR GeneID; 8623443; -.
DR KEGG; ddi:DDB_G0282141; -.
DR dictyBase; DDB_G0282141; hatA.
DR eggNOG; ENOG502RI2J; Eukaryota.
DR HOGENOM; CLU_2077490_0_0_1; -.
DR InParanoid; P13231; -.
DR PhylomeDB; P13231; -.
DR EvolutionaryTrace; P13231; -.
DR PRO; PR:P13231; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0003785; F:actin monomer binding; TAS:dictyBase.
DR GO; GO:0005504; F:fatty acid binding; IDA:dictyBase.
DR GO; GO:0008289; F:lipid binding; IDA:dictyBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:InterPro.
DR GO; GO:0030041; P:actin filament polymerization; IDA:dictyBase.
DR CDD; cd00257; Fascin; 1.
DR InterPro; IPR008999; Actin-crosslinking.
DR InterPro; IPR022768; Fascin-domain.
DR Pfam; PF06268; Fascin; 2.
DR SUPFAM; SSF50405; SSF50405; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Lipoprotein; Membrane;
KW Myristate; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..118
FT /note="Hisactophilin-1"
FT /id="PRO_0000083904"
FT REPEAT 34..46
FT /note="1"
FT REPEAT 74..86
FT /note="2"
FT REGION 8..109
FT /note="Contains several HHXH repeats"
FT REGION 34..86
FT /note="2 X 13 AA approximate repeats"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:7822284"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 68..79
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1HCD"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1HCE"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1HCD"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1HCD"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1HCD"
SQ SEQUENCE 118 AA; 13456 MW; B5B43F527B694716 CRC64;
MGNRAFKSHH GHFLSAEGEA VKTHHGHHDH HTHFHVENHG GKVALKTHCG KYLSIGDHKQ
VYLSHHLHGD HSLFHLEHHG GKVSIKGHHH HYISADHHGH VSTKEHHDHD TTFEEIII
