ID B9A025_HUMAN Unreviewed; 586 AA. AC B9A025; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 16-JAN-2019, entry version 71. DE SubName: Full=Lysyl oxidase homolog 3 {ECO:0000313|Ensembl:ENSP00000386545}; GN Name=LOXL3 {ECO:0000313|Ensembl:ENSP00000386545}; 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:ENSP00000386545, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000386545, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [2] {ECO:0000313|Ensembl:ENSP00000386545} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}. 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; AC005033; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005041; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; B9A025; -. DR jPOST; B9A025; -. DR PeptideAtlas; B9A025; -. DR PRIDE; B9A025; -. DR Ensembl; ENST00000409986; ENSP00000386545; ENSG00000115318. DR UCSC; uc010ffn.3; human. DR EuPathDB; HostDB:ENSG00000115318.11; -. DR HGNC; HGNC:13869; LOXL3. DR OpenTargets; ENSG00000115318; -. DR GeneTree; ENSGT00940000158157; -. DR HOGENOM; HOG000220841; -. DR HOVERGEN; HBG052336; -. DR ChiTaRS; LOXL3; human. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000115318; Expressed in 160 organ(s), highest expression level in tibia. DR ExpressionAtlas; B9A025; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016641; F:oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor; IEA:InterPro. DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro. DR Gene3D; 3.10.250.10; -; 3. DR InterPro; IPR001695; Lysyl_oxidase. DR InterPro; IPR019828; Lysyl_oxidase_CS. DR InterPro; IPR001190; SRCR. DR InterPro; IPR017448; SRCR-like_dom. DR InterPro; IPR036772; SRCR-like_dom_sf. DR Pfam; PF01186; Lysyl_oxidase; 1. DR Pfam; PF00530; SRCR; 3. DR PRINTS; PR00074; LYSYLOXIDASE. DR PRINTS; PR00258; SPERACTRCPTR. DR SMART; SM00202; SR; 3. DR SUPFAM; SSF56487; SSF56487; 3. DR PROSITE; PS00926; LYSYL_OXIDASE; 1. DR PROSITE; PS00420; SRCR_1; 1. DR PROSITE; PS50287; SRCR_2; 3. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00196, KW ECO:0000256|SAAS:SAAS00873970}; KW Proteomics identification {ECO:0000213|MaxQB:B9A025, KW ECO:0000213|PeptideAtlas:B9A025}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 586 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002879409. FT DOMAIN 44 145 SRCR. {ECO:0000259|PROSITE:PS50287}. FT DOMAIN 162 262 SRCR. {ECO:0000259|PROSITE:PS50287}. FT DOMAIN 272 380 SRCR. {ECO:0000259|PROSITE:PS50287}. FT DISULFID 70 134 {ECO:0000256|PROSITE-ProRule:PRU00196}. FT DISULFID 83 144 {ECO:0000256|PROSITE-ProRule:PRU00196}. FT DISULFID 114 124 {ECO:0000256|PROSITE-ProRule:PRU00196}. FT DISULFID 187 251 {ECO:0000256|PROSITE-ProRule:PRU00196}. FT DISULFID 200 261 {ECO:0000256|PROSITE-ProRule:PRU00196}. FT DISULFID 231 241 {ECO:0000256|PROSITE-ProRule:PRU00196}. FT DISULFID 347 357 {ECO:0000256|PROSITE-ProRule:PRU00196}. SQ SEQUENCE 586 AA; 64847 MW; 558E5D6C0061ED4D CRC64; MRPVSVWQWS PWGLLLCLLC SSCLGSPSPS TGPEKKAGSQ GLRFRLAGFP RKPYEGRVEI QRAGEWGTIC DDDFTLQAAH ILCRELGFTE ATGWTHSAKY GPGTGRIWLD NLSCSGTEQS VTECASRGWG NSDCTHDEDA GVICKDQRLP GFSDSNVIEA RVRLKGGAHP GEGRVEVLKA STWGTVCDRK WDLHAASVVC RELGFGSARE ALSGARMGQG MGAIHLSEVR CSGQELSLWK CPHKNITAED CSHSQDAGVR CNLPYTGAET RIRLSGGRSQ HEGRVEVQIG GPGPLRWGLI CGDDWGTLEA MVACRQLGLG YANHGLQETW YWDSGNITEV VMSGVRCTGT ELSLDQCAHH GTHITCKRTG TRFTAGVICS ETASDLLLHS ALVQETAYIE DRPLHMLYCA AEENCLASSA RSANWPYGHR RLLRFSSQIH NLGRADFRPK AGRHSWVWHE CHGHYHSMDI FTHYDILTPN GTKVAEGHKA SFCLEDTECQ EDVSKRYECA NFGEQGITVG CWDLYRHDID CQWIDITDVK PGNYILQVVI NPNFEVAESD FTNNAMKCNC KYDGHRIWVH NCHIGI //