ID A0A1B0GU92_HUMAN Unreviewed; 557 AA. AC A0A1B0GU92; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 16-JAN-2019, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSP00000490014}; 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 {ECO:0000313|Ensembl:ENSP00000490014, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000490014, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000490014} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the peptidase A1 family. CC {ECO:0000256|PROSITE-ProRule:PRU01103, CC ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS01079896}. 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; AC068580; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR BioMuta; ENSG00000250644; -. DR EPD; A0A1B0GU92; -. DR jPOST; A0A1B0GU92; -. DR Ensembl; ENST00000636615; ENSP00000490014; ENSG00000250644. DR GeneCards; ENSG00000250644; -. DR OpenTargets; ENSG00000250644; -. DR GeneTree; ENSGT00940000155733; -. DR Proteomes; UP000005640; Chromosome 11. DR ExpressionAtlas; A0A1B0GU92; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule. DR Gene3D; 2.40.70.10; -; 2. DR InterPro; IPR001461; Aspartic_peptidase_A1. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR012848; Aspartic_peptidase_N. DR InterPro; IPR007593; CD225/Dispanin_fam. DR InterPro; IPR033121; PEPTIDASE_A1. DR InterPro; IPR021109; Peptidase_aspartic_dom_sf. DR PANTHER; PTHR13683; PTHR13683; 1. DR Pfam; PF07966; A1_Propeptide; 1. DR Pfam; PF00026; Asp; 1. DR Pfam; PF04505; CD225; 1. DR PRINTS; PR00792; PEPSIN. DR SUPFAM; SSF50630; SSF50630; 1. DR PROSITE; PS00141; ASP_PROTEASE; 2. DR PROSITE; PS51767; PEPTIDASE_A1; 1. PE 1: Evidence at protein level; KW Aspartyl protease {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|RuleBase:RU000454}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|SAAS:SAAS00670207}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|RuleBase:RU000454}; Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|RuleBase:RU000454}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A1B0GU92}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 557 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008408637. FT TRANSMEM 482 507 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 528 550 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 79 404 Peptidase A1. FT {ECO:0000259|PROSITE:PS51767}. FT ACT_SITE 97 97 {ECO:0000256|PROSITE-ProRule:PRU01103}. FT ACT_SITE 295 295 {ECO:0000256|PROSITE-ProRule:PRU01103}. FT DISULFID 329 364 {ECO:0000256|PROSITE-ProRule:PRU01103}. SQ SEQUENCE 557 AA; 59860 MW; DCE4D24435E522A7 CRC64; MQPSSLLPLA LCLLAAPASA LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKAQG PGQCPAPLGD PASTTDGAQE ARVPLDGAFW IPRPPAGSPK GCFACVSKPP ALQAPAAPAP EPSASPPMAP TLFPMESKSS KTDSVRAAGA PPACKHLAEK KTMTNPTTVI EVYPDTTEVN DYYLWSIFNF VYLNFCCLGF IALAYSLKVR DKKLLNDLNG AVEDAKTARL FNITSSALAA SCIILVFIFL RYPLTDY //