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Q9Z175

- LOXL3_MOUSE

UniProt

Q9Z175 - LOXL3_MOUSE

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Protein

Lysyl oxidase homolog 3

Gene
Loxl3, Lor2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Copper By similarity.
Contains 1 lysine tyrosylquinone By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi608 – 6081Copper Reviewed prediction
Metal bindingi610 – 6101Copper Reviewed prediction
Metal bindingi612 – 6121Copper Reviewed prediction

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

Secretedextracellular space Reviewed prediction

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the lysyl oxidase family.
Contains 4 SRCR domains.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti347 – 3471R → P in AAC83205. 1 Publication

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

« 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: July 9, 2014
This is version 119 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