ID   A1CF_PONAB              Reviewed;         587 AA.
AC   Q5R9H4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=APOBEC1 complementation factor;
DE   AltName: Full=APOBEC1-stimulating protein;
GN   Name=A1CF; Synonyms=ACF;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1] {ECO:0000312|EMBL:CAH91586.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential component of the apolipoprotein B mRNA editing
CC       enzyme complex which is responsible for the postranscriptional editing
CC       of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to
CC       APOB mRNA and is probably responsible for docking the catalytic
CC       subunit, APOBEC1, to the mRNA to allow it to deaminate its target
CC       cytosine. The complex also seems to protect the edited APOB mRNA from
CC       nonsense-mediated decay (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NQ94}.
CC   -!- SUBUNIT: Part of the apolipoprotein B mRNA editing complex with
CC       APOBEC1. Interacts with TNPO2; TNPO2 may be responsible for transport
CC       of A1CF into the nucleus. Interacts with SYNCRIP. Interacts with
CC       CELF2/CUGBP2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly nuclear
CC       where it localizes to heterochromatin. Also cytoplasmic where it is
CC       found at the outer surface of the endoplasmic reticulum. Shuttles
CC       between the nucleus and cytoplasm. May be transported into the nucleus
CC       by the nuclear import protein TNPO2/TRN2 or by APOBEC1 (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The RRM domains are necessary but not sufficient for binding to
CC       APOB mRNA. Additional residues in the pre-RRM and C-terminal regions
CC       are required for RNA-binding and for complementing APOBEC1 activity (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NQ94}.
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DR   EMBL; CR859414; CAH91586.1; -; mRNA.
DR   RefSeq; NP_001127437.1; NM_001133965.1.
DR   AlphaFoldDB; Q5R9H4; -.
DR   SMR; Q5R9H4; -.
DR   STRING; 9601.ENSPPYP00000003286; -.
DR   GeneID; 100174508; -.
DR   KEGG; pon:100174508; -.
DR   CTD; 29974; -.
DR   eggNOG; KOG0117; Eukaryota.
DR   InParanoid; Q5R9H4; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0016556; P:mRNA modification; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   CDD; cd19900; DSRM_A1CF; 1.
DR   CDD; cd12486; RRM1_ACF; 1.
DR   CDD; cd12498; RRM3_ACF; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR033111; A1CF.
DR   InterPro; IPR044461; A1CF_DSRM.
DR   InterPro; IPR034538; ACF_RRM1.
DR   InterPro; IPR034539; ACF_RRM3.
DR   InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR21245:SF8; PTHR21245:SF8; 1.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; SSF54928; 3.
DR   TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; mRNA processing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..587
FT                   /note="APOBEC1 complementation factor"
FT                   /id="PRO_0000081484"
FT   DOMAIN          56..134
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          136..218
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          231..303
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          360..409
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ94"
FT   MOD_RES         491
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ94"
SQ   SEQUENCE   587 AA;  64380 MW;  162E011BA2CDF426 CRC64;
     MESNHKSGDG LSGTQKEAAL RALIQRTGYS LVQENGQRKY GGPPPGWDAA PPERGCEIFI
     GKLPRDLFED ELIPLCEKIG KIYEMRMMMD FNGNNRGYAF VTFSNKLEAK NAIKQLNNYE
     IRNGRLLGVC ASVDNCRLFV GGIPKTKKRE EILSEMKKVT EGVVDVIVYP SAADKTKNRG
     FAFVEYESHR AAAMARRKLL PGRIQLWGHP IAVDWAEPEV EVDEDTMSSV KILYVRNLML
     STSEEMIEKE FNNIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL
     AKPVDKDSYV RYTRGTGGRG TMLQGEYTYS LGQVYDPTTT YLGAPVFYAP QAYAAIPSLH
     FPATKGHLSN RAIIRAPSVR GAAGVRGLGG RGYLAYTGLG RGYQVKGDKR EDKLYDILPG
     MELTPMNPVT LKPQGIKLAP QILEEICQKN NWGQPVYQLH SAIGQDQRQL FLYKITIPAL
     ASQNPAIHPF TPPKLSAYVD EAKTYAAEYT LQTLGIPTDG GDAGTMATAA AVATAFPGYA
     VPNATAPVSA AQLKQAVTLG QDLAAYTTYE VYPTFAVTAR GDGYGAF