DLK1_RAT
ID DLK1_RAT Reviewed; 383 AA.
AC O70534; Q62779;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein delta homolog 1;
DE Short=DLK-1;
DE AltName: Full=Preadipocyte factor 1 {ECO:0000303|PubMed:9275085, ECO:0000303|PubMed:9645708};
DE Short=Pref-1;
DE Contains:
DE RecName: Full=Fetal antigen 1;
DE Short=FA1;
DE Flags: Precursor;
GN Name=Dlk1;
GN Synonyms=Dlk, Pref1 {ECO:0000303|PubMed:9275085,
GN ECO:0000303|PubMed:9645708}, Zog {ECO:0000303|PubMed:9645708};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Pancreatic islet;
RX PubMed=9275085; DOI=10.1210/endo.138.9.5408;
RA Carlsson C., Tornehave D., Lindberg K., Galante P., Billestrup N.,
RA Michelsen B., Larsson L.I., Nielsen J.H.;
RT "Growth hormone and prolactin stimulate the expression of rat preadipocyte
RT factor-1/delta-like protein in pancreatic islets: molecular cloning and
RT expression pattern during development and growth of the endocrine
RT pancreas.";
RL Endocrinology 138:3940-3948(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
RX PubMed=9645708; DOI=10.1210/endo.139.7.6081;
RA Halder S.K., Takemori H., Hatano O., Nonaka Y., Wada A., Okamoto M.;
RT "Cloning of a membrane-spanning protein with epidermal growth factor-like
RT repeat motifs from adrenal glomerulosa cells.";
RL Endocrinology 139:3316-3328(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 INTERACTION WITH SH3RF2.
RX PubMed=22128169; DOI=10.1074/jbc.m111.269431;
RA Wilhelm M., Kukekov N.V., Schmit T.L., Biagas K.V., Sproul A.A., Gire S.,
RA Maes M.E., Xu Z., Greene L.A.;
RT "Sh3rf2/POSHER protein promotes cell survival by RING-mediated proteasomal
RT degradation of the c-Jun N-terminal kinase scaffold POSH (Plenty of SH3s)
RT protein.";
RL J. Biol. Chem. 287:2247-2256(2012).
CC -!- FUNCTION: May have a role in neuroendocrine differentiation. Inhibits
CC adipocyte differentiation. {ECO:0000250|UniProtKB:Q09163}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with SH3RF2
CC (PubMed:22128169). {ECO:0000250|UniProtKB:Q09163,
CC ECO:0000269|PubMed:22128169}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein. Cytoplasm {ECO:0000269|PubMed:9645708}.
CC -!- TISSUE SPECIFICITY: Pancreas and adrenal glands (at protein level).
CC {ECO:0000269|PubMed:9275085, ECO:0000269|PubMed:9645708}.
CC -!- DEVELOPMENTAL STAGE: Embryonic pancreas and adrenal glands (at protein
CC level). {ECO:0000269|PubMed:9645708}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q09163}.
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DR EMBL; U25680; AAB87095.1; -; mRNA.
DR EMBL; D84336; BAA25881.1; -; mRNA.
DR EMBL; AABR07065528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07065529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC167752; AAI67752.1; -; mRNA.
DR RefSeq; NP_446196.1; NM_053744.1.
DR AlphaFoldDB; O70534; -.
DR SMR; O70534; -.
DR STRING; 10116.ENSRNOP00000006339; -.
DR iPTMnet; O70534; -.
DR PhosphoSitePlus; O70534; -.
DR PaxDb; O70534; -.
DR Ensembl; ENSRNOT00000085933; ENSRNOP00000069391; ENSRNOG00000019584.
DR GeneID; 114587; -.
DR KEGG; rno:114587; -.
DR CTD; 8788; -.
DR RGD; 619931; Dlk1.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000154225; -.
DR HOGENOM; CLU_039179_0_1_1; -.
DR InParanoid; O70534; -.
DR OMA; FNRCETW; -.
DR OrthoDB; 619882at2759; -.
DR PhylomeDB; O70534; -.
DR TreeFam; TF351835; -.
DR PRO; PR:O70534; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000019584; Expressed in stomach and 11 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IDA:RGD.
DR GO; GO:0048706; P:embryonic skeletal system development; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISO:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; 6.
DR PROSITE; PS50026; EGF_3; 6.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..383
FT /note="Protein delta homolog 1"
FT /id="PRO_5014306601"
FT CHAIN 24..303
FT /note="Fetal antigen 1"
FT /id="PRO_0000444802"
FT TOPO_DOM 24..306
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 24..55
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 59..86
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 88..125
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 127..168
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 170..206
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 208..245
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 26..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 30..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 45..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 63..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 76..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 92..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 97..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 115..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 131..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 138..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 158..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 174..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 179..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 196..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 212..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 217..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 235..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 273
FT /note="H -> Q (in Ref. 1; AAB87095)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="S -> R (in Ref. 1; AAB87095)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="G -> D (in Ref. 1; AAB87095)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="A -> G (in Ref. 1; AAB87095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 41149 MW; 123724C9801A9FD5 CRC64;
MIATGALLRV LLLLLAFGHS TYGAECDPAC DPQHGFCEAD NVCRCEPGWE GPLCEKCVTS
PGCVNGLCEE PWQCVCKEGW DGKFCEIDIR ACTSTPCANN GTCVDLEKGQ YECSCTPGFS
GKDCQHKAGP CVINGSPCQH GGACVDDEGR ASHASCLCPP GFSGNFCEIV TNSCTPNPCE
NDGVCTDIGG DFRCRCPAGF VDKTCSRPVS NCASGPCLNG GTCLQHTQVS FECLCKPPFM
GPTCAKKRGT SPVQVTHLPS GYGLTYRLTP GVHELPVQQP EHHILKVSMK ELNKSAPLLT
EGQAICFTIL GVLTSLVVLG TVAIVFLNKC EAWVSNLRYN HMLRKKKNLL LQYNSGEELA
VNIIFPEKID MTTFNKEAGD EDI
