EGLN_PIG
ID EGLN_PIG Reviewed; 653 AA.
AC P37176;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Endoglin;
DE AltName: CD_antigen=CD105;
DE Flags: Precursor;
GN Name=ENG;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH TGFB1 AND TGFB2.
RC TISSUE=Uterus;
RX PubMed=8294451; DOI=10.1016/s0021-9258(17)42126-0;
RA Yamashita H., Ichijo H., Grimsby S., Moren A., ten Dijke P., Miyazono K.;
RT "Endoglin forms a heteromeric complex with the signaling receptors for
RT transforming growth factor-beta.";
RL J. Biol. Chem. 269:1995-2001(1994).
CC -!- FUNCTION: Vascular endothelium glycoprotein that plays an important
CC role in the regulation of angiogenesis. Required for normal structure
CC and integrity of adult vasculature. Regulates the migration of vascular
CC endothelial cells (By similarity). Required for normal extraembryonic
CC angiogenesis and for embryonic heart development (By similarity). May
CC regulate endothelial cell shape changes in response to blood flow,
CC which drive vascular remodeling and establishment of normal vascular
CC morphology during angiogenesis (By similarity). May play a role in the
CC binding of endothelial cells to integrins (By similarity). Acts as TGF-
CC beta coreceptor and is involved in the TGF-beta/BMP signaling cascade
CC that ultimately leads to the activation of SMAD transcription factors
CC (PubMed:8294451). Required for GDF2/BMP9 signaling through SMAD1 in
CC endothelial cells and modulates TGFB1 signaling through SMAD3 (By
CC similarity). {ECO:0000250|UniProtKB:P17813,
CC ECO:0000250|UniProtKB:Q63961, ECO:0000269|PubMed:8294451}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms a heteromeric complex with
CC the signaling receptors for transforming growth factor-beta: TGFBR1
CC and/or TGFBR2. It is able to bind TGFB1 and TGFB2 with high affinity,
CC but not TGFB3 (PubMed:8294451). Interacts with GDF2, forming a
CC heterotetramer with a 2:2 stoichiometry. Interacts with ACVRL1. Can
CC form a heteromeric complex with GDF2 and ACVRL1. Interacts with BMP10.
CC Interacts with DYNLT4. Interacts with ARRB2 (By similarity).
CC {ECO:0000250|UniProtKB:P17813, ECO:0000269|PubMed:8294451}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8294451};
CC Single-pass type I membrane protein.
CC -!- DOMAIN: The ZP domain mediates dimerization.
CC {ECO:0000250|UniProtKB:P17813}.
CC -!- DOMAIN: The N-terminal OR region is composed of two intertwined domains
CC (OR1 and OR2) with a common, novel fold. Each contains 12 beta-strands
CC that form a parallel beta-helix-like structure, plus a single alpha-
CC helix. The OR1 region mediates interaction with GDF2.
CC {ECO:0000250|UniProtKB:P17813}.
CC -!- MISCELLANEOUS: Lacks a RGD motif, contrary to the human protein.
CC {ECO:0000305|PubMed:8294451}.
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DR EMBL; Z23142; CAA80673.1; -; mRNA.
DR PIR; A49722; A49722.
DR RefSeq; NP_999196.1; NM_214031.1.
DR AlphaFoldDB; P37176; -.
DR SMR; P37176; -.
DR STRING; 9823.ENSSSCP00000006026; -.
DR PaxDb; P37176; -.
DR PeptideAtlas; P37176; -.
DR PRIDE; P37176; -.
DR GeneID; 397096; -.
DR KEGG; ssc:397096; -.
DR CTD; 2022; -.
DR eggNOG; ENOG502RZQ9; Eukaryota.
DR InParanoid; P37176; -.
DR OrthoDB; 1263397at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:BHF-UCL.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; IBA:GO_Central.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IDA:BHF-UCL.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IDA:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IBA:GO_Central.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; IBA:GO_Central.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF00100; Zona_pellucida; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..653
FT /note="Endoglin"
FT /id="PRO_0000021158"
FT TOPO_DOM 25..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 362..512
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 27..336
FT /note="Required for interaction with GDF2"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 27..44
FT /note="OR1, N-terminal part"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 45..198
FT /note="OR2"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 199..329
FT /note="OR1, C-terminal part"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 269..281
FT /note="Essential for interaction with GDF2"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 625..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 641
FT /note="Phosphoserine; by TGFBR1"
FT /evidence="ECO:0000250|UniProtKB:Q63961"
FT MOD_RES 644
FT /note="Phosphoserine; by TGFBR1"
FT /evidence="ECO:0000250|UniProtKB:Q63961"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..206
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 51..181
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 241..329
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 349..381
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 362..442
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 393..411
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 493..549
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 516
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P17813"
SQ SEQUENCE 653 AA; 70280 MW; 7887B4A61DFE3E5A CRC64;
MDRGVLPQAI ALLLAVCSFG PTAGLAEGVQ CDLQPVDPKV TYTTSQVSEG CVAHVPNATV
GVHILFLEFS KEVSTLELTV QMTNPNGARP QEVLLILSVN KNIHLTLQVP EIPLHLAYDS
KLVFLQEAPK AVITELPPST TKNQLFLWAN TKGSIISAAE LDNPQSILLR LDQAPTSPSR
CTLEPRKDMG HTLEWKSHTQ ASVLGCHLEG VTGHKEAHIL RVLPGSEAWP RTVTVEVELS
CALRDPEAVL ILQGPPYVSW LIDANHNVKA WTTGEYSFKI FPGSNIQGVN LPDTRQGLLE
EARKLNASVI ASFVELPLAS VISLQDRSCG SGLQPSPTTV QITPPGEGCN QDLLLSLIQP
RCSDDVMTLV LRKDLISTLG CTITSLTFWD PSCQAEDTDD KFVLRGTYSS CGMKVAENVV
ISNEVVVNLL SSSSPQRKQV QCINLDSLSF QLGLYLSPHF LQASNTIELG QQGFVQVSMS
PSIPELMTQL DSCQLNLGPD VEMVDLIQNQ EAKSSCVSLL SPSPGGDMRF SFLLRGYVVP
MPTAGILSCT VALRPRTWSL DVHKTASTRL NIVSPGLPDK GLVLPAVLGI TFGAFLIGAL
LTAALWYIHS HTRHPGKREP VVAVAAPASS ESSSTNHSIG STQSTPCSTS SMA
