[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Swiss; TISSUE=Fibroblast; PubMed=8095043 [NCBI, ExPASy, EBI, Israel, Japan] Laborda J., Sausville E.A., Hoffman T., Notario V.; "dlk, a putative mammalian homeotic gene differentially expressed in small cell lung carcinoma and neuroendocrine tumor cell line."; J. Biol. Chem. 268:3817-3820(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0092-8674(93)90252-L; PubMed=8500166 [NCBI, ExPASy, EBI, Israel, Japan] Smas C.M., Sul H.S.; "Pref-1, a protein containing EGF-like repeats, inhibits adipocyte differentiation."; Cell 73:725-734(1993).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-347 DEL. TISSUE=Adrenal gland, and Placenta; PubMed=7711066 [NCBI, ExPASy, EBI, Israel, Japan] Lee Y.L., Helman L., Hoffman T., Laborda J.; "dlk, pG2 and Pref-1 mRNAs encode similar proteins belonging to the EGF-like superfamily. Identification of polymorphic variants of this RNA."; Biochim. Biophys. Acta 1261:223-232(1995).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. Maruyama K., Nishijima S., Kuromitsu S., Ichikawa A., Masuda E., Takemoto T., Kodama H., Kawashima H.; Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, AND ALTERNATIVE SPLICING. DOI=10.1021/bi00197a029; PubMed=7519443 [NCBI, ExPASy, EBI, Israel, Japan] Smas C.M., Green D., Sul H.S.; "Structural characterization and alternate splicing of the gene encoding the preadipocyte EGF-like protein pref-1."; Biochemistry 33:9257-9265(1994).
[6]	GLYCOSYLATION AT SER-94; ASN-100; ASN-165; ASN-174; SER-216; THR-224; THR-258; THR-267 AND THR-271, AND STRUCTURE OF CARBOHYDRATE. DOI=10.1111/j.1432-1033.1997.00334.x; PubMed=9118998 [NCBI, ExPASy, EBI, Israel, Japan] Krogh T.N., Bachmann E., Teisner B., Skjoedt K., Hoejrup P.; "Glycosylation analysis and protein structure determination of murine fetal antigen 1 (mFA1) -- the circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-derived protein 1 (SCP-1) cDNAs."; Eur. J. Biochem. 244:334-342(1997).

Comments

FUNCTION: May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation.
SUBUNIT: Monomer.
INTERACTION:
Q62406-1:Irak1; NbExp=2; IntAct=EBI-646470, EBI-488313;
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.

ALTERNATIVE PRODUCTS: 6 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.

Name	A
Isoform ID	Q09163-1
This is the isoform sequence displayed in this entry.

Name	B
Isoform ID	Q09163-2
Features which should be applied to build the isoform sequence: VSP_001380.

Name	C
Isoform ID	Q09163-3
Features which should be applied to build the isoform sequence: VSP_001381.

Name	C2
Isoform ID	Q09163-4
Features which should be applied to build the isoform sequence: VSP_001382.

Name	D
Isoform ID	Q09163-5
Features which should be applied to build the isoform sequence: VSP_001378.

Name	D2
Isoform ID	Q09163-6
Features which should be applied to build the isoform sequence: VSP_001379.

PTM: N- and O-glycosylated.
SIMILARITY: Contains 6 EGF-like domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z12171; CAA78162.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U15980; AAB60495.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L12721; AAA37175.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S71340; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
D16847; BAA04121.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00121716; -.
IPI00226664; -.
IPI00226665; -.
IPI00321359; -.
IPI00399832; -.
IPI00918517; -.

PIR

A54785; A54785.
S53718; S53718.

UniGene

Mm.157069

3D structure databases

HSSP

P00740; 1EDM. [HSSP ENTRY / PDB]

ModBase

Q09163.

Protein-protein interaction databases

DIP

DIP:6010N; -.

IntAct

Q09163; 1.

PTM databases

GlycoSuiteDB

Q09163; -.

Organism-specific databases

MGI

MGI:94900; Dlk1.

Gene expression databases

Q09163; -.

Q09163; -.

MM_DLK1; -.

ENSMUSG00000040856; Mus musculus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0048706;	Biological process: embryonic skeletal system development (inferred from direct assay from MGI).
GO:0009791;	Biological process: post-embryonic development (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR006209; EGF.
IPR006210; EGF-like.
IPR013032; EGF-like_reg_CS.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR001438; EGF_2.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
Graphical view of domain structure.

Pfam

PF00008; EGF; 4.
Pfam graphical view of domain structure.

PRINTS

PR00010; EGFBLOOD.

SMART

SM00181; EGF; 5.
SM00179; EGF_CA; 1.
SMART graphical view of domain structure.

PROSITE

PS00010; ASX_HYDROXYL; 1.
PS00022; EGF_1; 5.
PS01186; EGF_2; 6.
PS50026; EGF_3; 6.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000040856; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

Q09163; -.

HOVERGEN

Q09163; -.

Other

Dlk1; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Repeat; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`By similarity.`
`CHAIN`	`24 385`	`362`	`Protein delta homolog 1.`	`PRO_0000007520`
`CHAIN`	`24 305`	`282`	`Fetal antigen 1.`	`PRO_0000007521`
`TOPO_DOM`	`24 305`	`282`	`Extracellular (Potential).`
`TRANSMEM`	`306 329`	`24`	`Potential.`
`TOPO_DOM`	`330 385`	`56`	`Cytoplasmic (Potential).`
`DOMAIN`	`24 55`	`32`	`EGF-like 1.`
`DOMAIN`	`53 86`	`34`	`EGF-like 2.`
`DOMAIN`	`88 125`	`38`	`EGF-like 3.`
`DOMAIN`	`127 168`	`42`	`EGF-like 4.`
`DOMAIN`	`172 208`	`37`	`EGF-like 5.`
`DOMAIN`	`210 247`	`38`	`EGF-like 6.`
`CARBOHYD`	`94 94`		`O-linked (GalNAc...) [GlycoSuiteDB].`	`CAR_000160`
`CARBOHYD`	`100 100`		`N-linked (GlcNAc...) [GlycoSuiteDB].`	`CAR_000183`
`CARBOHYD`	`165 165`		`N-linked (GlcNAc...); partial; atypical.`
`CARBOHYD`	`174 174`		`N-linked (GlcNAc...); atypical.`
`CARBOHYD`	`216 216`		`O-linked (GalNAc...) [GlycoSuiteDB].`	`CAR_000161`
`CARBOHYD`	`224 224`		`O-linked (GalNAc...) [GlycoSuiteDB].`	`CAR_000162`
`CARBOHYD`	`258 258`		`O-linked (GalNAc...).`
`CARBOHYD`	`267 267`		`O-linked (GalNAc...); partial.`
`CARBOHYD`	`271 271`		`O-linked (GalNAc...).`
`CARBOHYD`	`295 295`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`26 37`		`By similarity.`
`DISULFID`	`30 43`		`By similarity.`
`DISULFID`	`45 54`		`By similarity.`
`DISULFID`	`57 68`		`By similarity.`
`DISULFID`	`63 74`		`By similarity.`
`DISULFID`	`76 85`		`By similarity.`
`DISULFID`	`92 103`		`By similarity.`
`DISULFID`	`97 113`		`By similarity.`
`DISULFID`	`115 124`		`By similarity.`
`DISULFID`	`131 144`		`By similarity.`
`DISULFID`	`138 156`		`By similarity.`
`DISULFID`	`158 167`		`By similarity.`
`DISULFID`	`176 187`		`By similarity.`
`DISULFID`	`181 196`		`By similarity.`
`DISULFID`	`198 207`		`By similarity.`
`DISULFID`	`214 225`		`By similarity.`
`DISULFID`	`219 235`		`By similarity.`
`DISULFID`	`237 246`		`By similarity.`
`VAR_SEQ`	`211 305`		`Missing (in isoform D2).`	`VSP_001379`
`VAR_SEQ`	`211 303`		`Missing (in isoform D).`	`VSP_001378`
`VAR_SEQ`	`231 305`		`Missing (in isoform C2).`	`VSP_001382`
`VAR_SEQ`	`231 303`		`Missing (in isoform C).`	`VSP_001381`
`VAR_SEQ`	`231 281`		`Missing (in isoform B).`	`VSP_001380`
`VARIANT`	`347 347`	`1`	`Missing.`
`CONFLICT`	`250 250`		`R -> P (in Ref. 2; AAA37175).`
`CONFLICT`	`320 385`		`VLGTVAIVFLNKCETWVSNLRYNHTFRKKKNLLLQYNSGE` `ELAVNIIFPEKIDMTTFNKEAGDEEI -> CWAPWPSSFSTSAKPGCPTCATTTCFARRRTSCCSITAAR` `SWRSISSSPRRLT (in Ref. 2; AAA37175).`
`CONFLICT`	`344 345`		`TF -> ML (in Ref. 4; BAA04121).`

Sequence information

Length: 385 AA [This is the length of the unprocessed precursor]

Molecular weight: 41320 Da [This is the MW of the unprocessed precursor]

CRC64: E79864FEA5AF4FF1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIATGALLRV LLLLLAFGHS TYGAECDPPC DPQYGFCEAD NVCRCHVGWE GPLCDKCVTA 

        70         80         90        100        110        120 
PGCVNGVCKE PWQCICKDGW DGKFCEIDVR ACTSTPCANN GTCVDLEKGQ YECSCTPGFS 

       130        140        150        160        170        180 
GKDCQHKAGP CVINGSPCQH GGACVDDEGQ ASHASCLCPP GFSGNFCEIV AATNSCTPNP 

       190        200        210        220        230        240 
CENDGVCTDI GGDFRCRCPA GFVDKTCSRP VSNCASGPCQ NGGTCLQHTQ VSFECLCKPP 

       250        260        270        280        290        300 
FMGPTCAKKR GASPVQVTHL PSGYGLTYRL TPGVHELPVQ QPEQHILKVS MKELNKSTPL 

       310        320        330        340        350        360 
LTEGQAICFT ILGVLTSLVV LGTVAIVFLN KCETWVSNLR YNHTFRKKKN LLLQYNSGEE 

       370        380 
LAVNIIFPEK IDMTTFNKEA GDEEI

Q09163 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools