Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lysyl oxidase homolog 3

Gene

Loxl3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Cofactori

Protein has several cofactor binding sites:

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
Complete GO annotation...

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 region Source: MGI
  2. extracellular space Source: UniProtKB-SubCell
  3. membrane Source: InterPro
Complete GO annotation...

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

MaxQBiQ9Z175.
PRIDEiQ9Z175.

PTM databases

PhosphoSiteiQ9Z175.

Expressioni

Gene expression databases

BgeeiQ9Z175.
CleanExiMM_LOXL3.
ExpressionAtlasiQ9Z175. baseline and differential.
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.
GeneTreeiENSGT00760000119251.
HOGENOMiHOG000220841.
HOVERGENiHBG052336.
InParanoidiQ9Z175.
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

        10         20         30         40         50
MRAVSVWYCC PWGLLLLHCL CSFSVGSPSP SISPEKKVGS QGLRFRLAGF
60 70 80 90 100
PRKPYEGRVE IQRAGEWGTI CDDDFTLQAA HVLCRELGFT EATGWTHSAK
110 120 130 140 150
YGPGTGRIWL DNLSCRGTEG SVTECASRGW GNSDCTHDED AGVICKDQRL
160 170 180 190 200
PGFSDSNVIE VEHQLQVEEV RLRPAVEWGR RPLPVTEGLV EVRLPEGWSQ
210 220 230 240 250
VCDKGWSAHN SHVVCGMLGF PGEKRVNMAF YRMLAQKKQH SFGLHSVACV
260 270 280 290 300
GTEAHLSLCS LEFYRANDTT RCSGGNPAVV SCVLGPLYAT FTGQKKQQHS
310 320 330 340 350
KPQGEARVRL KGGAHQGEGR VEVLKAGTWG TVCDRKWDLQ AASVVCRELG
360 370 380 390 400
FGTAREALSG ARMGQGMGAI HLSEVRCSGQ EPSLWRCPSK NITAEDCSHS
410 420 430 440 450
QDAGVRCNLP YTGVETKIRL SGGRSRYEGR VEVQIGIPGH LRWGLICGDD
460 470 480 490 500
WGTLEAMVAC RQLGLGYANH GLQETWYWDS GNVTEVVMSG VRCTGSELSL
510 520 530 540 550
NQCAHHSSHI TCKKTGTRFT AGVICSETAS DLLLHSALVQ ETAYIEDRPL
560 570 580 590 600
HMLYCAAEEN CLASSARSAN WPYGHRRLLR FSSQIHNLGR ADFRPKAGRH
610 620 630 640 650
SWVWHECHGH YHSMDIFTHY DILTPNGTKV AEGHKASFCL EDTECQEDVS
660 670 680 690 700
KRYECANFGE QGITVGCWDL YRHDIDCQWI DITDVKPGNY ILQVVINPNF
710 720 730 740 750
EVAESDFTNN AMKCNCKYDG HRIWVHNCHI GDAFSEEANR RFERYPGQTS

NQIV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiQ9Z175. 1 interaction.
STRINGi10090.ENSMUSP00000000707.

PTM databases

PhosphoSiteiQ9Z175.

Proteomic databases

MaxQBiQ9Z175.
PRIDEiQ9Z175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi84695.
MGIiMGI:1337004. Loxl3.

Phylogenomic databases

eggNOGiNOG40770.
GeneTreeiENSGT00760000119251.
HOGENOMiHOG000220841.
HOVERGENiHBG052336.
InParanoidiQ9Z175.
KOiK00280.
OMAiTWYWDSG.
OrthoDBiEOG7SN8C6.
TreeFamiTF326061.

Miscellaneous databases

NextBioi291000.
PROiQ9Z175.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z175.
CleanExiMM_LOXL3.
ExpressionAtlasiQ9Z175. baseline and differential.
GenevestigatoriQ9Z175.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 124 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.