YJEN3_HUMAN
ID YJEN3_HUMAN Reviewed; 299 AA.
AC A6XGL0; A6XGK9; Q4G1C0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=YjeF N-terminal domain-containing protein 3 {ECO:0000305};
DE Short=YjeF_N3;
DE Short=hYjeF_N3;
DE AltName: Full=ApoA-I-binding protein 2 {ECO:0000250|UniProtKB:Q1LVI2};
GN Name=YJEFN3; Synonyms=AIBP2 {ECO:0000250|UniProtKB:Q1LVI2};
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] (ISOFORMS 1 AND 2).
RA Yu Z., Zheng Z., Tang T., Fu Y.;
RT "A computer system platform used to predict novel genes and some proteins
RT similar to apolipoprotein a1 binding protein.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17533573; DOI=10.1055/s-2007-977699;
RA Rudolph C., Sigruener A., Hartmann A., Orso E., Bals-Pratsch M.,
RA Gronwald W., Seifert B., Kalbitzer H.R., Verdorfer I., Luetjens C.M.,
RA Ortmann O., Bornstein S.R., Schmitz G.;
RT "ApoA-I-binding protein (AI-BP) and its homologues hYjeF_N2 and hYjeF_N3
RT comprise the YjeF_N domain protein family in humans with a role in
RT spermiogenesis and oogenesis.";
RL Horm. Metab. Res. 39:322-335(2007).
RN [6]
RP INTERACTION WITH APOA1.
RX PubMed=23719382; DOI=10.1038/nature12166;
RA Fang L., Choi S.H., Baek J.S., Liu C., Almazan F., Ulrich F., Wiesner P.,
RA Taleb A., Deer E., Pattison J., Torres-Vazquez J., Li A.C., Miller Y.I.;
RT "Control of angiogenesis by AIBP-mediated cholesterol efflux.";
RL Nature 498:118-122(2013).
CC -!- FUNCTION: May accelerate cholesterol efflux from endothelial cells to
CC high-density lipoprotein (HDL) and thereby regulates angiogenesis. May
CC orchestrate hematopoietic stem and progenitor cell emergence from the
CC hemogenic endothelium, a type of specialized endothelium manifesting
CC hematopoietic potential. YJEFN3-mediated cholesterol efflux activates
CC endothelial SREBF2, the master transcription factor for cholesterol
CC biosynthesis, which in turn transactivates NOTCH and promotes
CC hematopoietic stem and progenitor cell emergence (By similarity). May
CC play a role in spermiogenesis and oogenesis (PubMed:17533573).
CC {ECO:0000250|UniProtKB:Q1LVI2, ECO:0000269|PubMed:17533573}.
CC -!- SUBUNIT: Interacts with APOA1 (PubMed:23719382). Binds to HDL
CC (PubMed:17533573). {ECO:0000269|PubMed:17533573,
CC ECO:0000269|PubMed:23719382}.
CC -!- INTERACTION:
CC A6XGL0; P28062-2: PSMB8; NbExp=3; IntAct=EBI-13070200, EBI-372312;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6XGL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6XGL0-2; Sequence=VSP_035170;
CC -!- TISSUE SPECIFICITY: Expressed in theca cells in ovary and in Leydig
CC cells in testis (at protein level). Also expressed in brain and mammary
CC gland. {ECO:0000269|PubMed:17533573}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC020948; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ778080; ABI63344.1; -; mRNA.
DR EMBL; DQ778079; ABI63349.1; -; mRNA.
DR EMBL; AC011448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84827.1; -; Genomic_DNA.
DR EMBL; BC020948; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS42530.1; -. [A6XGL0-1]
DR CCDS; CCDS54236.1; -. [A6XGL0-2]
DR RefSeq; NP_001177257.1; NM_001190328.1. [A6XGL0-2]
DR RefSeq; NP_940939.2; NM_198537.3. [A6XGL0-1]
DR AlphaFoldDB; A6XGL0; -.
DR SMR; A6XGL0; -.
DR BioGRID; 131931; 16.
DR IntAct; A6XGL0; 1.
DR STRING; 9606.ENSP00000426964; -.
DR iPTMnet; A6XGL0; -.
DR PhosphoSitePlus; A6XGL0; -.
DR BioMuta; YJEFN3; -.
DR MassIVE; A6XGL0; -.
DR PaxDb; A6XGL0; -.
DR PeptideAtlas; A6XGL0; -.
DR PRIDE; A6XGL0; -.
DR ProteomicsDB; 1760; -. [A6XGL0-1]
DR ProteomicsDB; 1761; -. [A6XGL0-2]
DR Antibodypedia; 54853; 8 antibodies from 6 providers.
DR DNASU; 374887; -.
DR Ensembl; ENST00000436027.9; ENSP00000398520.2; ENSG00000250067.12. [A6XGL0-2]
DR Ensembl; ENST00000514277.6; ENSP00000426964.1; ENSG00000250067.12. [A6XGL0-1]
DR GeneID; 374887; -.
DR KEGG; hsa:374887; -.
DR MANE-Select; ENST00000514277.6; ENSP00000426964.1; NM_198537.4; NP_940939.2.
DR UCSC; uc002nmt.3; human. [A6XGL0-1]
DR CTD; 374887; -.
DR DisGeNET; 374887; -.
DR GeneCards; YJEFN3; -.
DR HGNC; HGNC:24785; YJEFN3.
DR HPA; ENSG00000250067; Group enriched (brain, testis).
DR MIM; 618607; gene.
DR neXtProt; NX_A6XGL0; -.
DR OpenTargets; ENSG00000250067; -.
DR PharmGKB; PA164727608; -.
DR VEuPathDB; HostDB:ENSG00000250067; -.
DR eggNOG; KOG2585; Eukaryota.
DR GeneTree; ENSGT00390000007227; -.
DR HOGENOM; CLU_024853_3_0_1; -.
DR InParanoid; A6XGL0; -.
DR OMA; NIKEPYP; -.
DR OrthoDB; 1030667at2759; -.
DR PhylomeDB; A6XGL0; -.
DR TreeFam; TF300197; -.
DR PathwayCommons; A6XGL0; -.
DR SignaLink; A6XGL0; -.
DR BioGRID-ORCS; 374887; 66 hits in 1076 CRISPR screens.
DR ChiTaRS; YJEFN3; human.
DR GenomeRNAi; 374887; -.
DR Pharos; A6XGL0; Tdark.
DR PRO; PR:A6XGL0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; A6XGL0; protein.
DR Bgee; ENSG00000250067; Expressed in putamen and 96 other tissues.
DR ExpressionAtlas; A6XGL0; baseline and differential.
DR Genevisible; A6XGL0; HS.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052856; F:NADHX epimerase activity; IBA:GO_Central.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0031580; P:membrane raft distribution; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0010874; P:regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR Gene3D; 3.40.50.10260; -; 1.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR InterPro; IPR032976; YJEFN_prot_NAXE-like.
DR PANTHER; PTHR13232; PTHR13232; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF64153; SSF64153; 1.
DR TIGRFAMs; TIGR00197; yjeF_nterm; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid transport; Reference proteome; Transport.
FT CHAIN 1..299
FT /note="YjeF N-terminal domain-containing protein 3"
FT /id="PRO_0000348461"
FT DOMAIN 74..287
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00719"
FT VAR_SEQ 20..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_035170"
FT VARIANT 213
FT /note="A -> T (in dbSNP:rs58031491)"
FT /id="VAR_061989"
FT CONFLICT 293
FT /note="T -> A (in Ref. 4; BC020948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 32585 MW; 5B708900DEBF6CCE CRC64;
MSSAAGPDPS EAPEERHFLR ALELQPPLAD MGRAELSSNA TTSLVQRRKQ AWGRQSWLEQ
IWNAGPVCQS TAEAAALERE LLEDYRFGRQ QLVELCGHAS AVAVTKAFPL PALSRKQRTV
LVVCGPEQNG AVGLVCARHL RVFEYEPTIF YPTRSLDLLH RDLTTQCEKM DIPFLSYLPT
EVQLINEAYG LVVDAVLGPG VEPGEVGGPC TRALATLKLL SIPLVSLDIP SGWDAETGSD
SEDGLRPDVL VSLAAPKRCA GRFSGRHHFV AGRFVPDDVR RKFALRLPGY TGTDCVAAL
