ID   ACL7A_RAT               Reviewed;         440 AA.
AC   Q641W9;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Actin-like protein 7A;
GN   Name=Actl7a;
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   INTERACTION WITH TES AND ENAH, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=21278383; DOI=10.1074/jbc.m110.171264;
RA   Boeda B., Knowles P.P., Briggs D.C., Murray-Rust J., Soriano E.,
RA   Garvalov B.K., McDonald N.Q., Way M.;
RT   "Molecular recognition of the Tes LIM2-3 domains by the actin-related
RT   protein Arp7A.";
RL   J. Biol. Chem. 286:11543-11554(2011).
CC   -!- FUNCTION: May play an important role in formation and fusion of Golgi-
CC       derived vesicles during acrosome biogenesis.
CC       {ECO:0000250|UniProtKB:Q9QY84}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with TES (via LIM domain 2).
CC       Heterodimer with TES; the heterodimer interacts with ENAH to form a
CC       heterotrimer (PubMed:21278383). Interacts with ACTL9 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y615, ECO:0000269|PubMed:21278383}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9QY84}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q9QY84}. Cytoplasm
CC       {ECO:0000269|PubMed:21278383}. Nucleus {ECO:0000250|UniProtKB:Q9QY84}.
CC       Note=Detected at the Golgi apparatus during acrosome biogenesis.
CC       Detected at the subacrosomal layer in round spermatids. Detected in
CC       sperm head and tail. {ECO:0000250|UniProtKB:Q9QY84}.
CC   -!- TISSUE SPECIFICITY: Detected in testis. Detected at the acrosome of
CC       round spermatids (at protein level). {ECO:0000269|PubMed:21278383}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; BC082101; AAH82101.1; -; mRNA.
DR   RefSeq; NP_001011973.1; NM_001011973.1.
DR   RefSeq; XP_008761929.1; XM_008763707.2.
DR   AlphaFoldDB; Q641W9; -.
DR   SMR; Q641W9; -.
DR   IntAct; Q641W9; 1.
DR   STRING; 10116.ENSRNOP00000022395; -.
DR   PhosphoSitePlus; Q641W9; -.
DR   PaxDb; Q641W9; -.
DR   PRIDE; Q641W9; -.
DR   Ensembl; ENSRNOT00000022395; ENSRNOP00000022395; ENSRNOG00000016641.
DR   GeneID; 298017; -.
DR   KEGG; rno:298017; -.
DR   UCSC; RGD:1304697; rat.
DR   CTD; 10881; -.
DR   RGD; 1304697; Actl7a.
DR   eggNOG; KOG0676; Eukaryota.
DR   GeneTree; ENSGT00940000162158; -.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; Q641W9; -.
DR   OMA; MNNSGKH; -.
DR   OrthoDB; 964605at2759; -.
DR   PhylomeDB; Q641W9; -.
DR   TreeFam; TF354237; -.
DR   PRO; PR:Q641W9; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000016641; Expressed in testis and 10 other tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001673; C:male germ cell nucleus; ISO:RGD.
DR   GO; GO:0031514; C:motile cilium; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0001675; P:acrosome assembly; ISS:UniProtKB.
DR   GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR027679; ACTL7A.
DR   InterPro; IPR031769; ACTL7A_N.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF167; PTHR11937:SF167; 1.
DR   Pfam; PF00022; Actin; 1.
DR   Pfam; PF16840; ACTL7A_N; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Fertilization; Golgi apparatus; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..440
FT                   /note="Actin-like protein 7A"
FT                   /id="PRO_0000282829"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          36..56
FT                   /note="Required for interaction with TES"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y615"
SQ   SEQUENCE   440 AA;  49568 MW;  EE38C1EA8098D653 CRC64;
     MSLDAVWAPQ TANIGDGPAK KASDQTSMQT QVLQTASLRD GPAKRAVWVR RDNAEKEEPV
     KSAVSKDRPR LEVTKAVVVD LGTGFCKCGF AGLPKPTHKI STTVGKPYME TAKTGDNRKE
     TFVGRELFNP DIHLKLVNPL RHGIIVDWDT VQDIWEYLFR QEMKIAPEEH AVLVSDPPLS
     PHTNREKYAE MLFETFNTPA MHIAYQSRLS MYSYGRTSGL VVEVGHGVSY VVPIYEGYPL
     PSITGRLDYA GSDLTNYLMN LMNNCGKHFS EDHLSIVEDI KTKCCFVALD PIEEKKIPPS
     EHEIHYTLPD GKEIRLGQER FLCSEMFFKP SLIKSMQLGL HTQTVSCLNK CDIALKRDLM
     GNILLCGGST MLRGFPNRLQ KELSSMCPND TPQVNVLPER DTAVWTGGSI LASLQGFQPL
     WVHRLEYEEH GPFFLYRRCF