ACTN_DERFA
ID ACTN_DERFA Reviewed; 885 AA.
AC L7UZ85;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Alpha-actinin {ECO:0000303|PubMed:24324688};
DE AltName: Full=F-actin cross-linking protein {ECO:0000305};
DE AltName: Allergen=Der f 24 {ECO:0000303|PubMed:24324688};
OS Dermatophagoides farinae (American house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX NCBI_TaxID=6954;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 263-286; 489-496; 502-511;
RP 513-524; 700-710; 722-733; 737-747 AND 844-856, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND ALLERGEN.
RX PubMed=24324688; DOI=10.1371/journal.pone.0081377;
RA An S., Shen C., Liu X., Chen L., Xu X., Rong M., Liu Z., Lai R.;
RT "Alpha-actinin is a new type of house dust mite allergen.";
RL PLoS ONE 8:E81377-E81377(2013).
CC -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC actin to a variety of intracellular structures. This is a bundling
CC protein. {ECO:0000250|UniProtKB:P18091}.
CC -!- SUBUNIT: Homodimer; antiparallel. {ECO:0000250|UniProtKB:P35609}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. Activates
CC basophils. {ECO:0000269|PubMed:24324688}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; KC305498; AGC56214.1; -; mRNA.
DR AlphaFoldDB; L7UZ85; -.
DR SMR; L7UZ85; -.
DR Allergome; 11748; Der f Actinin.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00150; SPEC; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Allergen; Calcium; Direct protein sequencing; Metal-binding;
KW Repeat.
FT CHAIN 1..885
FT /note="Alpha-actinin"
FT /id="PRO_0000439247"
FT DOMAIN 26..130
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 139..245
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 270..377
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 389..494
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 508..614
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 626..727
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT DOMAIN 741..776
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 780..815
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..242
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT BINDING 754
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 758
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 760
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 765
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 793
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 797
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 885 AA; 103319 MW; 3D5A08FCF848643F CRC64;
MTQDGYMQQE EEEWEREGLL DPAWEKQQRK TFTAWCNSHL RKAGTQIDNI EEDFRNGLKL
MLLLEVISGE TLGKPDRGKM RFHKIANVNK ALDFIESKGV KLVSIGAEEI VDGNSKMTLG
LIWTIILRFA IQDISVEEMT AKEGLLLWCQ RKTAPYKNVN VQNFHLSWKD GLAFCALIHR
HRPDLIDYGK LRKDNPMDNF NLAFDVAEKH LNIPRMLDAE DVVYTAKPDE RAIMTYVSWY
YHAFHGAQQA ETAANRICKV LKVNQDNERL MEEYERLASD LLEWIRRTTP WLENRTTDNT
LPGTQKKLEE FRSYRRQHKP PRVEQKANLE TNFNTLQTKL RLSKRPAYMP SEGKMVSDIT
GAWKGLESAE KGFEEWLLSE MMRLERLDHL AQKFKHKADI HEEWTQGKEE MLVSHDFRQC
KLNEIKALKK KHEAFESDLA AHQDRVEQIA AIAQELNALG YHDIASINAR CQRICDQWDR
LGTLTTRRRQ ALDEAEQILE KVDLFHLEFA KRAAPFNNWL DETREDLVDM FIVHSIEEIQ
QLIDAHESFK NTLGEADKEY KTIVGLAQEV QPMATQYQIP GGLENPYTTL TPEVITTKWR
DVKQLVPQRD HTLQTELIRQ QCNENLRRQF AEKANVVGPW IERQMDAVTA IGMGMQGTLE
DQLQRLHEYD QAVVQYRPHV DDLEKIHQEV QEAMIFENRY TQYTMETLRV GWEQLLTSIH
RNINEVENQI LTRDSKGITQ EQLNEFRTSF NHFDKKRTGR LAPEEFKSCL VSLGYNIRND
DRPEFRRILA IVDPNKTGYV HFDAFLDFMT REYTDTDTAE QMIDSFRILA GDKPYITADE
LRRELPPDQA EYCIRRMTPY NGQCAVPGAL DYRSFSTALY GESDL
