ID   A0A1B0GU03_HUMAN        Unreviewed;       582 AA.
AC   A0A1B0GU03;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   13-FEB-2019, entry version 16.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSP00000489910};
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:ENSP00000489910, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000489910, 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:ENSP00000489910}
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   SMR; A0A1B0GU03; -.
DR   BioMuta; ENSG00000250644; -.
DR   jPOST; A0A1B0GU03; -.
DR   PeptideAtlas; A0A1B0GU03; -.
DR   Ensembl; ENST00000636397; ENSP00000489910; ENSG00000250644.
DR   GeneCards; ENSG00000250644; -.
DR   OpenTargets; ENSG00000250644; -.
DR   GeneTree; ENSGT00940000155733; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   ExpressionAtlas; A0A1B0GU03; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:A0A1B0GU03};
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    582       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008408623.
FT   TRANSMEM    482    505       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   582 AA;  62702 MW;  943253CC53F6C074 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 IALAYSLKPR LEWPRPDVLH QCSCPAGWGR RQGMQGEKRL
     GRGWLGGRTP GQLRLCSILE LEPHPARHRN CGRRSPPAPD SS
//