POTEF_HUMAN
ID POTEF_HUMAN Reviewed; 1075 AA.
AC A5A3E0; A6NC34;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=POTE ankyrin domain family member F;
DE AltName: Full=ANKRD26-like family C member 1B;
DE AltName: Full=Chimeric POTE-actin protein;
GN Name=POTEF; Synonyms=A26C1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Mammary cancer;
RX PubMed=17101985; DOI=10.1073/pnas.0608344103;
RA Lee Y., Ise T., Ha D., Saint Fleur A., Hahn Y., Liu X.-F., Nagata S.,
RA Lee B., Bera T.K., Pastan I.;
RT "Evolution and expression of chimeric POTE-actin genes in the human
RT genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17885-17890(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:17101985}. Note=Colocalizes with actin filaments.
CC -!- TISSUE SPECIFICITY: Expressed in breast cancer cell lines (at protein
CC level). {ECO:0000269|PubMed:17101985}.
CC -!- MISCELLANEOUS: Results from the insertion of a beta-actin fragment at
CC the C-terminus in the POTEE paralog gene leading to the formation of a
CC new functional chimeric protein. This insertion occured before the
CC divergence of the Old World monkeys and apes.
CC -!- SIMILARITY: In the N-terminal section; belongs to the POTE family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the actin family.
CC {ECO:0000305}.
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DR EMBL; EF523384; ABP57734.1; -; mRNA.
DR EMBL; AC018804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS46409.1; -.
DR RefSeq; NP_001093241.1; NM_001099771.2.
DR AlphaFoldDB; A5A3E0; -.
DR SMR; A5A3E0; -.
DR BioGRID; 608805; 299.
DR IntAct; A5A3E0; 64.
DR MINT; A5A3E0; -.
DR STRING; 9606.ENSP00000350052; -.
DR GlyGen; A5A3E0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A5A3E0; -.
DR PhosphoSitePlus; A5A3E0; -.
DR SwissPalm; A5A3E0; -.
DR BioMuta; POTEF; -.
DR EPD; A5A3E0; -.
DR jPOST; A5A3E0; -.
DR MassIVE; A5A3E0; -.
DR MaxQB; A5A3E0; -.
DR PaxDb; A5A3E0; -.
DR PeptideAtlas; A5A3E0; -.
DR PRIDE; A5A3E0; -.
DR ProteomicsDB; 705; -.
DR Antibodypedia; 56072; 121 antibodies from 10 providers.
DR DNASU; 728378; -.
DR Ensembl; ENST00000409914.7; ENSP00000386786.2; ENSG00000196604.13.
DR GeneID; 728378; -.
DR KEGG; hsa:728378; -.
DR MANE-Select; ENST00000409914.7; ENSP00000386786.2; NM_001099771.2; NP_001093241.1.
DR UCSC; uc010fmh.3; human.
DR CTD; 728378; -.
DR DisGeNET; 728378; -.
DR GeneCards; POTEF; -.
DR HGNC; HGNC:33905; POTEF.
DR HPA; ENSG00000196604; Group enriched (brain, testis).
DR neXtProt; NX_A5A3E0; -.
DR OpenTargets; ENSG00000196604; -.
DR PharmGKB; PA164724818; -.
DR VEuPathDB; HostDB:ENSG00000196604; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000163068; -.
DR HOGENOM; CLU_010163_0_0_1; -.
DR InParanoid; A5A3E0; -.
DR OMA; CARNHAR; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; A5A3E0; -.
DR TreeFam; TF354237; -.
DR PathwayCommons; A5A3E0; -.
DR SignaLink; A5A3E0; -.
DR BioGRID-ORCS; 728378; 69 hits in 991 CRISPR screens.
DR GenomeRNAi; 728378; -.
DR Pharos; A5A3E0; Tbio.
DR PRO; PR:A5A3E0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; A5A3E0; protein.
DR Bgee; ENSG00000196604; Expressed in testis and 16 other tissues.
DR ExpressionAtlas; A5A3E0; baseline and differential.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR039497; CC144C-like_CC_dom.
DR Pfam; PF00022; Actin; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF14915; CCDC144C; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW ANK repeat; Coiled coil; Cytoplasm; Reference proteome; Repeat.
FT CHAIN 1..1075
FT /note="POTE ankyrin domain family member F"
FT /id="PRO_0000307859"
FT REPEAT 172..201
FT /note="ANK 1"
FT REPEAT 205..234
FT /note="ANK 2"
FT REPEAT 238..267
FT /note="ANK 3"
FT REPEAT 271..300
FT /note="ANK 4"
FT REPEAT 304..333
FT /note="ANK 5"
FT REGION 369..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..1075
FT /note="Actin-like"
FT COILED 399..435
FT /evidence="ECO:0000255"
FT COILED 642..698
FT /evidence="ECO:0000255"
FT COMPBIAS 378..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 4
FT /note="E -> G (in Ref. 1; ABP57734)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="S -> L (in Ref. 1; ABP57734)"
FT /evidence="ECO:0000305"
FT CONFLICT 930
FT /note="V -> A (in Ref. 1; ABP57734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1075 AA; 121445 MW; 8833FF435D1B6902 CRC64;
MVVEVDSMPA ASSVKKPFGL RSKMGKWCCR CFPCCRESGK SNVGTSGDHD DSAMKTLRSK
MGKWCRHCFP CCRGSGKSNV GASGDHDDSA MKTLRNKMGK WCCHCFPCCR GSSKSKVGAW
GDYDDSAFME PRYHVRGEDL DKLHRAAWWG KVPRKDLIVM LRDTDVNKQD KQKRTALHLA
SANGNSEVVK LLLDRRCQLN VLDNKKRTAL IKAVQCQEDE CALMLLEHGT DPNIPDEYGN
TTLHYAIYNE DKLMAKALLL YGADIESKNK HGLTPLLLGV HEQKQQVVKF LIKKKANLNA
LDRYGRTALI LAVCCGSASI VSLLLEQNID VSSQDLSGQT AREYAVSSHH HVICQLLSDY
KEKQMLKISS ENSNPEQDLK LTSEEESQRF KGSENSQPEK MSQEPEINKD GDREVEEEMK
KHESNNVGLL ENLTNGVTAG NGDNGLIPQR KSRTPENQQF PDNESEEYHR ICELLSDYKE
KQMPKYSSEN SNPEQDLKLT SEEESQRLKG SENGQPEKRS QEPEINKDGD RELENFMAIE
EMKKHRSTHV GFPENLTNGA TAGNGDDGLI PPRKSRTPES QQFPDTENEE YHSDEQNDTQ
KQFCEEQNTG ILHDEILIHE EKQIEVVEKM NSELSLSCKK EKDILHENST LREEIAMLRL
ELDTMKHQSQ LREKKYLEDI ESVKKRNDNL LKALQLNELT MDDDTAVLVI DNGSGMCKAG
FAGDDAPRAV FPSIVGRPRQ QGMMGGMHQK ESYVGKEAQS KRGILTLKYP MEHGIITNWD
DMEKIWHHTF YNELRVAPEE HPVLLTEATL NPKANREKMT QIMFETFNTP AMYVAIQAVL
SLYTSGRTTG IVMDSGDGVT HTVPIYEGNA LPHATLRLDL AGRELPDYLM KILTEHGYRF
TTMAEREIVR DIKEKLCYVA LDFEQEMATV ASSSSLEKSY ELPDGQVITI GNERFRCPEA
LFQPCFLGME SCGIHETTFN SIMKSDVDIR KDLYTNTVLS GGTTMYPGMA HRMQKEIAAL
APSMMKIRII APPKRKYSVW VGGSILASLS TFQQMWISKQ EYDESGPSIV HRKCL
