ID Q6FH22_HUMAN Unreviewed; 443 AA. AC Q6FH22; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 18-JUN-2025, entry version 125. DE RecName: Full=EGF-containing fibulin-like extracellular matrix protein 2 {ECO:0000256|ARBA:ARBA00072845}; DE AltName: Full=Fibulin-4 {ECO:0000256|ARBA:ARBA00080306}; GN Name=EFEMP2 {ECO:0000313|EMBL:CAG46732.1}; 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 {ECO:0000313|EMBL:CAG46732.1}; RN [1] {ECO:0000313|EMBL:CAG46732.1} RP NUCLEOTIDE SEQUENCE. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays a crucial role in elastic fiber formation in tissue, CC and in the formation of ultrastructural connections between elastic CC laminae and smooth muscle cells in the aorta, therefore participates in CC terminal differentiation and maturation of smooth muscle cell (SMC) and CC in the mechanical properties and wall integrity maintenance of the CC aorta. In addition, is involved in the control of collagen fibril CC assembly in tissue throught proteolytic activation of LOX leading to CC cross- linking of collagen and elastin. Also promotes ELN coacervation CC and participates in the deposition of ELN coacervates on to CC microfibrils but also regulates ELN cross- linking through LOX CC interaction. Moreover adheres to the cells through heparin binding in a CC calcium-dependent manner and regulates vascularlar smooth muscle cells CC proliferation through angiotensin signaling. CC {ECO:0000256|ARBA:ARBA00053851}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}. CC -!- SIMILARITY: Belongs to the fibulin family. CC {ECO:0000256|ARBA:ARBA00006127}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR541934; CAG46732.1; -; mRNA. DR AlphaFoldDB; Q6FH22; -. DR IntAct; Q6FH22; 1. DR PeptideAtlas; Q6FH22; -. DR OrthoDB; 4062651at2759; -. DR ChiTaRS; EFEMP2; human. DR GO; GO:0031012; C:extracellular matrix; IEA:UniProtKB-ARBA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR CDD; cd00054; EGF_CA; 2. DR FunFam; 2.10.25.10:FF:000201; EGF-containing fibulin-like extracellular matrix protein 2; 1. DR FunFam; 2.10.25.10:FF:000290; EGF-containing fibulin-like extracellular matrix protein 2; 1. DR FunFam; 2.10.25.10:FF:000366; EGF-containing fibulin-like extracellular matrix protein 2; 1. DR FunFam; 2.10.25.10:FF:000367; EGF-containing fibulin-like extracellular matrix protein 2; 1. DR FunFam; 2.10.25.10:FF:000210; Hemicentin 1; 1. DR FunFam; 2.10.25.10:FF:000014; Latent-transforming growth factor beta-binding protein 3; 1. DR Gene3D; 2.10.25.10; Laminin; 6. DR InterPro; IPR026823; cEGF. 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 InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR055088; Fibulin_C. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR052235; Nephronectin_domain. DR InterPro; IPR049883; NOTCH1_EGF-like. DR PANTHER; PTHR24050; PA14 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24050:SF28; UROMODULIN-LIKE; 1. DR Pfam; PF12662; cEGF; 2. DR Pfam; PF07645; EGF_CA; 3. DR Pfam; PF22914; Fibulin_C; 1. DR Pfam; PF12661; hEGF; 1. DR PRINTS; PR00907; THRMBOMODULN. DR SMART; SM00181; EGF; 5. DR SMART; SM00179; EGF_CA; 6. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 4. DR PROSITE; PS01186; EGF_2; 3. DR PROSITE; PS50026; EGF_3; 3. DR PROSITE; PS01187; EGF_CA; 2. PE 2: Evidence at transcript level; KW Basement membrane {ECO:0000256|ARBA:ARBA00022869}; KW Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE- KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..443 FT /note="EGF-containing fibulin-like extracellular matrix FT protein 2" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004274557" FT DOMAIN 123..163 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 164..202 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 243..282 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" SQ SEQUENCE 443 AA; 49391 MW; 14BACCD739603DB6 CRC64; MLPCASCLPG SLLLWALLLL LLGSASPQDS EEPDSYTECT DGYEWDPDSQ HCRDVNECLT IPEACKGEMK CINHYGGYLC LPRSAAVIND LHGEGPPPPV PPAQHPNPCP PGYEPDDQDS CVDVDECAQA LHDCRPSQDC HNLPGSYQCT CPDGYRKIGP ECVDIDECRY RYCQHRCVNL PGSFRCQCEP GFQLGPNNRS CVDVNECDMG APCEQRCFNS YGTFLCRCHQ GYELHRDGFS CSDIDECSYS SYLCQYRCVN EPGRFSCHCP QGYQLLATRL CQDIDECESG AHQCSEAQTC VNFHGGYRCV DTNRCVEPYI QVSENRCLCP ASNPLCREQP SSIVHRYMTI TSKRSVPADV FQIQATSVYP GAYNAFQIRA GNSQGDFYIR QINNVSAMLV LARPVTGPRE YVLDLEMVTM NSLMSYRASS VLRLTVFVGA YTF //