GenomeNet

Database: UniProt
Entry: P80370
LinkDB: P80370
Original site: P80370 
ID   DLK1_HUMAN              Reviewed;         383 AA.
AC   P80370; P15803; Q96DW5;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   13-FEB-2019, entry version 191.
DE   RecName: Full=Protein delta homolog 1;
DE            Short=DLK-1;
DE   AltName: Full=pG2;
DE   Contains:
DE     RecName: Full=Fetal antigen 1;
DE              Short=FA1;
DE   Flags: Precursor;
GN   Name=DLK1; Synonyms=DLK;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANTS GLY-101 AND
RP   GLY-108.
RC   TISSUE=Adrenal gland;
RX   PubMed=8095043;
RA   Laborda J., Sausville E.A., Hoffman T., Notario V.;
RT   "dlk, a putative mammalian homeotic gene differentially expressed in
RT   small cell lung carcinoma and neuroendocrine tumor cell line.";
RL   J. Biol. Chem. 268:3817-3820(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND VARIANTS
RP   GLY-101 AND GLY-108.
RC   TISSUE=Adrenal gland, and Placenta;
RX   PubMed=7711066;
RA   Lee Y.L., Helman L., Hoffman T., Laborda J.;
RT   "dlk, pG2 and Pref-1 mRNAs encode similar proteins belonging to the
RT   EGF-like superfamily. Identification of polymorphic variants of this
RT   RNA.";
RL   Biochim. Biophys. Acta 1261:223-232(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT GLY-101.
RC   TISSUE=Adrenal gland;
RX   PubMed=2308864; DOI=10.1093/nar/18.3.685;
RA   Helman L.J., Sack N., Plon S., Israel M.A.;
RT   "The sequence of an adrenal specific human cDNA, pG2.";
RL   Nucleic Acids Res. 18:685-685(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANT
RP   GLY-101.
RC   TISSUE=Adrenal gland;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 24-383, GLYCOSYLATION AT SER-94; ASN-100; THR-143;
RP   SER-163; ASN-165; ASN-172; SER-214; THR-222; SER-251 AND SER-260, AND
RP   VARIANT GLY-101.
RC   TISSUE=Amniotic fluid;
RX   PubMed=7925474; DOI=10.1111/j.1432-1033.1994.00083.x;
RA   Jensen C.H., Krogh T.N., Hoejrup P., Clausen P.P., Skjoedt K.,
RA   Larsson L.-I., Enghild J.J., Teisner B.;
RT   "Protein structure of fetal antigen 1 (FA1). A novel circulating human
RT   epidermal-growth-factor-like protein expressed in neuroendocrine
RT   tumors and its relation to the gene products of dlk and pG2.";
RL   Eur. J. Biochem. 225:83-92(1994).
RN   [7]
RP   PROTEIN SEQUENCE OF 24-60.
RC   TISSUE=Amniotic fluid;
RX   PubMed=8501199;
RA   Jensen C.H., Teisner B., Hoejrup P., Rasmussen H.B., Madsen O.D.,
RA   Nielsen B., Skjoedt K.;
RT   "Studies on the isolation, structural analysis and tissue localization
RT   of fetal antigen 1 and its relation to a human adrenal-specific cDNA,
RT   pG2.";
RL   Hum. Reprod. 8:635-641(1993).
RN   [8]
RP   PROTEIN SEQUENCE OF 24-38.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [9]
RP   GLYCOSYLATION AT THR-256, STRUCTURE OF CARBOHYDRATES, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22171320; DOI=10.1074/mcp.M111.013649;
RA   Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT   "Human urinary glycoproteomics; attachment site specific analysis of
RT   N-and O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
CC   -!- FUNCTION: May have a role in neuroendocrine differentiation.
CC   -!- SUBUNIT: Monomer. Interacts with SH3RF2 (By similarity).
CC       {ECO:0000250|UniProtKB:O70534}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Cytoplasm {ECO:0000250|UniProtKB:O70534}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=Long;
CC         IsoId=P80370-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P80370-2; Sequence=VSP_001377;
CC   -!- TISSUE SPECIFICITY: Found within the stromal cells in close
CC       contact to the vascular structure of placental villi, yolk sac,
CC       fetal liver, adrenal cortex and pancreas and in the beta cells of
CC       the islets of Langerhans in the adult pancreas. Found also in some
CC       forms of neuroendocrine lung tumor tissue.
CC   -!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly
CC       core 8 glycans. {ECO:0000269|PubMed:22171320,
CC       ECO:0000269|PubMed:7925474}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA35582.1; Type=Frameshift; Positions=22, 108, 199; Evidence={ECO:0000305};
DR   EMBL; Z12172; CAA78163.1; -; mRNA.
DR   EMBL; U15979; AAA75364.1; -; mRNA.
DR   EMBL; U15981; AAA75365.1; -; mRNA.
DR   EMBL; X17544; CAA35582.1; ALT_FRAME; mRNA.
DR   EMBL; AL132711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013197; AAH13197.1; -; mRNA.
DR   CCDS; CCDS81852.1; -. [P80370-2]
DR   CCDS; CCDS9963.1; -. [P80370-1]
DR   PIR; S53716; S53716.
DR   PIR; S71548; S71548.
DR   RefSeq; NP_001304101.1; NM_001317172.1.
DR   RefSeq; NP_003827.3; NM_003836.6.
DR   UniGene; Hs.116631; -.
DR   UniGene; Hs.533717; -.
DR   ProteinModelPortal; P80370; -.
DR   SMR; P80370; -.
DR   BioGrid; 114316; 72.
DR   STRING; 9606.ENSP00000340292; -.
DR   BindingDB; P80370; -.
DR   ChEMBL; CHEMBL5671; -.
DR   GlyConnect; 745; -.
DR   iPTMnet; P80370; -.
DR   PhosphoSitePlus; P80370; -.
DR   UniCarbKB; P80370; -.
DR   BioMuta; DLK1; -.
DR   DMDM; 296439371; -.
DR   PaxDb; P80370; -.
DR   PeptideAtlas; P80370; -.
DR   PRIDE; P80370; -.
DR   ProteomicsDB; 57681; -.
DR   ProteomicsDB; 57682; -. [P80370-2]
DR   DNASU; 8788; -.
DR   Ensembl; ENST00000331224; ENSP00000331081; ENSG00000185559. [P80370-2]
DR   Ensembl; ENST00000341267; ENSP00000340292; ENSG00000185559. [P80370-1]
DR   Ensembl; ENST00000650464; ENSP00000497700; ENSG00000185559. [P80370-1]
DR   GeneID; 8788; -.
DR   KEGG; hsa:8788; -.
DR   UCSC; uc001yhs.5; human. [P80370-1]
DR   CTD; 8788; -.
DR   DisGeNET; 8788; -.
DR   EuPathDB; HostDB:ENSG00000185559.13; -.
DR   GeneCards; DLK1; -.
DR   H-InvDB; HIX0131238; -.
DR   HGNC; HGNC:2907; DLK1.
DR   HPA; CAB005872; -.
DR   HPA; HPA053879; -.
DR   HPA; HPA062262; -.
DR   MalaCards; DLK1; -.
DR   MIM; 176290; gene.
DR   neXtProt; NX_P80370; -.
DR   OpenTargets; ENSG00000185559; -.
DR   Orphanet; 169615; Idiopathic central precocious puberty.
DR   Orphanet; 254534; Kagami-Ogata syndrome due to maternal 14q32.2 hypermethylation.
DR   Orphanet; 254528; Kagami-Ogata syndrome due to maternal 14q32.2 microdeletion.
DR   Orphanet; 96334; Kagami-Ogata syndrome due to paternal uniparental disomy of chromosome 14.
DR   Orphanet; 96184; Temple syndrome due to maternal uniparental disomy of chromosome 14.
DR   Orphanet; 254531; Temple syndrome due to paternal 14q32.2 hypomethylation.
DR   Orphanet; 254525; Temple syndrome due to paternal 14q32.2 microdeletion.
DR   PharmGKB; PA27363; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   GeneTree; ENSGT00940000154225; -.
DR   HOGENOM; HOG000072581; -.
DR   HOVERGEN; HBG007065; -.
DR   InParanoid; P80370; -.
DR   OMA; WLANAKY; -.
DR   OrthoDB; 311898at2759; -.
DR   PhylomeDB; P80370; -.
DR   TreeFam; TF351835; -.
DR   Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   SignaLink; P80370; -.
DR   SIGNOR; P80370; -.
DR   ChiTaRS; DLK1; human.
DR   GeneWiki; DLK1; -.
DR   GenomeRNAi; 8788; -.
DR   PRO; PR:P80370; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000185559; Expressed in 157 organ(s), highest expression level in metanephros.
DR   ExpressionAtlas; P80370; baseline and differential.
DR   Genevisible; P80370; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:HGNC.
DR   GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:HGNC.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   Pfam; PF00008; EGF; 4.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Polymorphism; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000269|PubMed:15340161,
FT                                ECO:0000269|PubMed:7925474,
FT                                ECO:0000269|PubMed:8501199}.
FT   CHAIN        24    383       Protein delta homolog 1.
FT                                /FTId=PRO_0000007518.
FT   CHAIN        24    303       Fetal antigen 1.
FT                                /FTId=PRO_0000007519.
FT   TOPO_DOM     24    303       Extracellular. {ECO:0000255}.
FT   TRANSMEM    304    327       Helical. {ECO:0000255}.
FT   TOPO_DOM    328    383       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       24     55       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       53     86       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       88    125       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      127    168       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      170    206       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      208    245       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     94     94       O-linked (GalNAc...) serine.
FT                                {ECO:0000269|PubMed:7925474}.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:7925474}.
FT   CARBOHYD    143    143       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:7925474}.
FT   CARBOHYD    163    163       O-linked (GalNAc...) serine; partial.
FT                                {ECO:0000269|PubMed:7925474}.
FT   CARBOHYD    165    165       N-linked (GlcNAc...) asparagine;
FT                                atypical; partial.
FT                                {ECO:0000269|PubMed:7925474}.
FT   CARBOHYD    172    172       N-linked (GlcNAc...) asparagine;
FT                                atypical; partial.
FT                                {ECO:0000269|PubMed:7925474}.
FT   CARBOHYD    214    214       O-linked (GalNAc...) serine.
FT                                {ECO:0000269|PubMed:7925474}.
FT   CARBOHYD    222    222       O-linked (GalNAc...) threonine; partial.
FT                                {ECO:0000269|PubMed:7925474}.
FT   CARBOHYD    251    251       O-linked (GalNAc...) serine; partial.
FT                                {ECO:0000269|PubMed:7925474}.
FT   CARBOHYD    256    256       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:22171320}.
FT   CARBOHYD    260    260       O-linked (GalNAc...) serine; partial.
FT                                {ECO:0000269|PubMed:7925474}.
FT   DISULFID     26     37       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     30     43       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     45     54       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     57     68       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     63     74       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     76     85       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     92    103       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     97    113       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    115    124       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    131    144       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    138    156       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    158    167       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    174    185       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    179    194       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    196    205       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    212    223       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    217    233       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    235    244       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     229    301       Missing (in isoform Short).
FT                                {ECO:0000303|PubMed:7711066}.
FT                                /FTId=VSP_001377.
FT   VARIANT      73     73       Q -> L (in dbSNP:rs34686110).
FT                                /FTId=VAR_055715.
FT   VARIANT     101    101       R -> G (in dbSNP:rs6575799).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:2308864,
FT                                ECO:0000269|PubMed:7711066,
FT                                ECO:0000269|PubMed:7925474,
FT                                ECO:0000269|PubMed:8095043}.
FT                                /FTId=VAR_060335.
FT   VARIANT     104    104       V -> M (in dbSNP:rs2273607).
FT                                /FTId=VAR_055716.
FT   VARIANT     108    108       D -> G (in dbSNP:rs1058006).
FT                                {ECO:0000269|PubMed:7711066,
FT                                ECO:0000269|PubMed:8095043}.
FT                                /FTId=VAR_060336.
FT   VARIANT     260    260       S -> N (in dbSNP:rs1058009).
FT                                /FTId=VAR_055717.
FT   VARIANT     347    347       Missing.
FT                                /FTId=VAR_002274.
FT   CONFLICT     45     47       Missing (in Ref. 3; CAA35582).
FT                                {ECO:0000305}.
FT   CONFLICT     46     47       QP -> HV (in Ref. 1; CAA78163).
FT                                {ECO:0000305}.
SQ   SEQUENCE   383 AA;  41300 MW;  9A2813B2801A98BD CRC64;
     MTATEALLRV LLLLLAFGHS TYGAECFPAC NPQNGFCEDD NVCRCQPGWQ GPLCDQCVTS
     PGCLHGLCGE PGQCICTDGW DGELCDRDVR ACSSAPCANN RTCVSLDDGL YECSCAPGYS
     GKDCQKKDGP CVINGSPCQH GGTCVDDEGR ASHASCLCPP GFSGNFCEIV ANSCTPNPCE
     NDGVCTDIGG DFRCRCPAGF IDKTCSRPVT NCASSPCQNG GTCLQHTQVS YECLCKPEFT
     GLTCVKKRAL SPQQVTRLPS GYGLAYRLTP GVHELPVQQP EHRILKVSMK ELNKKTPLLT
     EGQAICFTIL GVLTSLVVLG TVGIVFLNKC ETWVSNLRYN HMLRKKKNLL LQYNSGEDLA
     VNIIFPEKID MTTFSKEAGD EEI
//
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