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Q9Z175

- LOXL3_MOUSE

UniProt

Q9Z175 - LOXL3_MOUSE

Protein

Lysyl oxidase homolog 3

Gene

Loxl3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Functions as amine oxidases toward elastin and different types of collagens.By similarity

    Cofactori

    Copper.By similarity
    Contains 1 lysine tyrosylquinone.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi608 – 6081CopperSequence Analysis
    Metal bindingi610 – 6101CopperSequence Analysis
    Metal bindingi612 – 6121CopperSequence Analysis

    GO - Molecular functioni

    1. copper ion binding Source: InterPro
    2. oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor Source: InterPro
    3. scavenger receptor activity Source: InterPro

    GO - Biological processi

    1. epithelial to mesenchymal transition Source: UniProtKB
    2. negative regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysyl oxidase homolog 3 (EC:1.4.3.-)
    Alternative name(s):
    Lysyl oxidase-like protein 3
    Lysyl oxidase-related protein 2
    Gene namesi
    Name:Loxl3
    Synonyms:Lor2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1337004. Loxl3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell
    2. membrane Source: InterPro

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 754728Lysyl oxidase homolog 3PRO_0000018534Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi71 ↔ 135PROSITE-ProRule annotation
    Disulfide bondi84 ↔ 145PROSITE-ProRule annotation
    Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi115 ↔ 125PROSITE-ProRule annotation
    Disulfide bondi202 ↔ 272PROSITE-ProRule annotation
    Disulfide bondi215 ↔ 282PROSITE-ProRule annotation
    Disulfide bondi249 ↔ 259PROSITE-ProRule annotation
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi333 ↔ 397PROSITE-ProRule annotation
    Disulfide bondi346 ↔ 407PROSITE-ProRule annotation
    Disulfide bondi377 ↔ 387PROSITE-ProRule annotation
    Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi447 ↔ 512PROSITE-ProRule annotation
    Disulfide bondi460 ↔ 525PROSITE-ProRule annotation
    Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi493 ↔ 503PROSITE-ProRule annotation
    Disulfide bondi555 ↔ 561PROSITE-ProRule annotation
    Disulfide bondi607 ↔ 655PROSITE-ProRule annotation
    Glycosylationi626 – 6261N-linked (GlcNAc...)Sequence Analysis
    Cross-linki635 ↔ 671Lysine tyrosylquinone (Lys-Tyr)By similarity
    Disulfide bondi639 ↔ 645PROSITE-ProRule annotation
    Disulfide bondi667 ↔ 677PROSITE-ProRule annotation
    Modified residuei671 – 67112',4',5'-topaquinoneBy similarity
    Disulfide bondi714 ↔ 728PROSITE-ProRule annotation

    Post-translational modificationi

    The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, LTQ, TPQ

    Proteomic databases

    PRIDEiQ9Z175.

    PTM databases

    PhosphoSiteiQ9Z175.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Z175.
    BgeeiQ9Z175.
    CleanExiMM_LOXL3.
    GenevestigatoriQ9Z175.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9Z175. 1 interaction.
    STRINGi10090.ENSMUSP00000000707.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z175.
    SMRiQ9Z175. Positions 57-145, 305-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 146102SRCR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini170 – 283114SRCR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini308 – 408101SRCR 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini418 – 526109SRCR 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni530 – 733204Lysyl-oxidase likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the lysyl oxidase family.Curated
    Contains 4 SRCR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG40770.
    GeneTreeiENSGT00740000115380.
    HOGENOMiHOG000220841.
    HOVERGENiHBG052336.
    InParanoidiQ91VN8.
    KOiK00280.
    OMAiTWYWDSG.
    OrthoDBiEOG7SN8C6.
    TreeFamiTF326061.

    Family and domain databases

    Gene3Di3.10.250.10. 4 hits.
    InterProiIPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view]
    PfamiPF01186. Lysyl_oxidase. 1 hit.
    PF00530. SRCR. 4 hits.
    [Graphical view]
    PRINTSiPR00074. LYSYLOXIDASE.
    PR00258. SPERACTRCPTR.
    SMARTiSM00202. SR. 4 hits.
    [Graphical view]
    SUPFAMiSSF56487. SSF56487. 4 hits.
    PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
    PS00420. SRCR_1. 1 hit.
    PS50287. SRCR_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Z175-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRAVSVWYCC PWGLLLLHCL CSFSVGSPSP SISPEKKVGS QGLRFRLAGF    50
    PRKPYEGRVE IQRAGEWGTI CDDDFTLQAA HVLCRELGFT EATGWTHSAK 100
    YGPGTGRIWL DNLSCRGTEG SVTECASRGW GNSDCTHDED AGVICKDQRL 150
    PGFSDSNVIE VEHQLQVEEV RLRPAVEWGR RPLPVTEGLV EVRLPEGWSQ 200
    VCDKGWSAHN SHVVCGMLGF PGEKRVNMAF YRMLAQKKQH SFGLHSVACV 250
    GTEAHLSLCS LEFYRANDTT RCSGGNPAVV SCVLGPLYAT FTGQKKQQHS 300
    KPQGEARVRL KGGAHQGEGR VEVLKAGTWG TVCDRKWDLQ AASVVCRELG 350
    FGTAREALSG ARMGQGMGAI HLSEVRCSGQ EPSLWRCPSK NITAEDCSHS 400
    QDAGVRCNLP YTGVETKIRL SGGRSRYEGR VEVQIGIPGH LRWGLICGDD 450
    WGTLEAMVAC RQLGLGYANH GLQETWYWDS GNVTEVVMSG VRCTGSELSL 500
    NQCAHHSSHI TCKKTGTRFT AGVICSETAS DLLLHSALVQ ETAYIEDRPL 550
    HMLYCAAEEN CLASSARSAN WPYGHRRLLR FSSQIHNLGR ADFRPKAGRH 600
    SWVWHECHGH YHSMDIFTHY DILTPNGTKV AEGHKASFCL EDTECQEDVS 650
    KRYECANFGE QGITVGCWDL YRHDIDCQWI DITDVKPGNY ILQVVINPNF 700
    EVAESDFTNN AMKCNCKYDG HRIWVHNCHI GDAFSEEANR RFERYPGQTS 750
    NQIV 754
    Length:754
    Mass (Da):83,740
    Last modified:July 27, 2011 - v2
    Checksum:iC3BF60F77696914D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti347 – 3471R → P in AAC83205. (PubMed:9927484)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053368 mRNA. Translation: AAC83205.1.
    AF084363 Genomic DNA. Translation: AAC95338.1.
    AK030548 mRNA. Translation: BAC27016.1.
    CH466523 Genomic DNA. Translation: EDK99047.1.
    BC011298 mRNA. Translation: AAH11298.1.
    CCDSiCCDS20266.1.
    RefSeqiNP_038614.2. NM_013586.4.
    UniGeneiMm.380433.

    Genome annotation databases

    EnsembliENSMUST00000000707; ENSMUSP00000000707; ENSMUSG00000000693.
    GeneIDi16950.
    KEGGimmu:16950.
    UCSCiuc009clt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053368 mRNA. Translation: AAC83205.1 .
    AF084363 Genomic DNA. Translation: AAC95338.1 .
    AK030548 mRNA. Translation: BAC27016.1 .
    CH466523 Genomic DNA. Translation: EDK99047.1 .
    BC011298 mRNA. Translation: AAH11298.1 .
    CCDSi CCDS20266.1.
    RefSeqi NP_038614.2. NM_013586.4.
    UniGenei Mm.380433.

    3D structure databases

    ProteinModelPortali Q9Z175.
    SMRi Q9Z175. Positions 57-145, 305-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Z175. 1 interaction.
    STRINGi 10090.ENSMUSP00000000707.

    PTM databases

    PhosphoSitei Q9Z175.

    Proteomic databases

    PRIDEi Q9Z175.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000707 ; ENSMUSP00000000707 ; ENSMUSG00000000693 .
    GeneIDi 16950.
    KEGGi mmu:16950.
    UCSCi uc009clt.1. mouse.

    Organism-specific databases

    CTDi 84695.
    MGIi MGI:1337004. Loxl3.

    Phylogenomic databases

    eggNOGi NOG40770.
    GeneTreei ENSGT00740000115380.
    HOGENOMi HOG000220841.
    HOVERGENi HBG052336.
    InParanoidi Q91VN8.
    KOi K00280.
    OMAi TWYWDSG.
    OrthoDBi EOG7SN8C6.
    TreeFami TF326061.

    Miscellaneous databases

    NextBioi 291000.
    PROi Q9Z175.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z175.
    Bgeei Q9Z175.
    CleanExi MM_LOXL3.
    Genevestigatori Q9Z175.

    Family and domain databases

    Gene3Di 3.10.250.10. 4 hits.
    InterProi IPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view ]
    Pfami PF01186. Lysyl_oxidase. 1 hit.
    PF00530. SRCR. 4 hits.
    [Graphical view ]
    PRINTSi PR00074. LYSYLOXIDASE.
    PR00258. SPERACTRCPTR.
    SMARTi SM00202. SR. 4 hits.
    [Graphical view ]
    SUPFAMi SSF56487. SSF56487. 4 hits.
    PROSITEi PS00926. LYSYL_OXIDASE. 1 hit.
    PS00420. SRCR_1. 1 hit.
    PS50287. SRCR_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparative sequence of human and mouse BAC clones from the mnd2 region of chromosome 2p13."
      Jang W., Hua A., Spilson S.V., Miller W., Roe B.A., Meisler M.H.
      Genome Res. 9:53-61(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: 129/SvJ and C57BL/6J.
      Tissue: Muscle.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Pituitary.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiLOXL3_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z175
    Secondary accession number(s): Q91VN8, Q9JJ39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3