Q96JB6 (LOXL4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysyl oxidase homolog 4
EC=1.4.3.-

Alternative name(s):
Lysyl oxidase-like protein 4
Lysyl oxidase-related protein C

Gene names

Name:	LOXL4
Synonyms:	LOXC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	756 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May modulate the formation of a collagenous extracellular matrix.
Cofactor	Copper By similarity. Contains 1 lysine tyrosylquinone By similarity.
Subcellular location	Secreted › extracellular space Potential.
Tissue specificity	Expressed in many tissues, the highest levels among the tissues studied being in the skeletal muscle, testis and pancreas. Expressed in cartilage.
Post-translational modification	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.
Sequence similarities	Belongs to the lysyl oxidase family. Contains 4 SRCR domains.
Sequence caution	The sequence AAH07522.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein LTQ Phosphoprotein TPQ
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct scavenger receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRIP13	Q15645	3	EBI-749562,EBI-358993

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 756	732	Lysyl oxidase homolog 4		PRO_0000018535
Regions
	Domain	32 – 133	102	SRCR 1
	Domain	159 – 287	129	SRCR 2
	Domain	311 – 411	101	SRCR 3
	Domain	421 – 529	109	SRCR 4
	Region	533 – 736	204	Lysyl-oxidase like
Sites
	Metal binding	611	1	Copper Potential
	Metal binding	613	1	Copper Potential
	Metal binding	615	1	Copper Potential
Amino acid modifications
	Modified residue	383	1	Phosphotyrosine Ref.8
	Modified residue	674	1	2',4',5'-topaquinone By similarity
	Glycosylation	198	1	N-linked (GlcNAc...) Potential
	Glycosylation	629	1	N-linked (GlcNAc...) Potential
	Disulfide bond	58 ↔ 122		By similarity
	Disulfide bond	71 ↔ 132		By similarity
	Disulfide bond	102 ↔ 112		By similarity
	Disulfide bond	191 ↔ 276		By similarity
	Disulfide bond	204 ↔ 286		By similarity
	Disulfide bond	251 ↔ 261		By similarity
	Disulfide bond	336 ↔ 400		By similarity
	Disulfide bond	349 ↔ 410		By similarity
	Disulfide bond	380 ↔ 390		By similarity
	Disulfide bond	450 ↔ 515		By similarity
	Disulfide bond	463 ↔ 528		By similarity
	Disulfide bond	497 ↔ 507		By similarity
	Disulfide bond	558 ↔ 564		By similarity
	Disulfide bond	610 ↔ 658		By similarity
	Disulfide bond	642 ↔ 648		By similarity
	Disulfide bond	670 ↔ 680		By similarity
	Disulfide bond	717 ↔ 731		By similarity
	Cross-link	638 ↔ 674		Lysine tyrosylquinone (Lys-Tyr) By similarity
Natural variations
	Natural variant	154	1	R → Q. Corresponds to variant rs33995374 [ dbSNP | Ensembl ].		VAR_050012
	Natural variant	372	1	P → T. Corresponds to variant rs11189525 [ dbSNP | Ensembl ].		VAR_059431
	Natural variant	405	1	D → A. Ref.7 Corresponds to variant rs1983864 [ dbSNP | Ensembl ].		VAR_050013
Experimental info
	Sequence conflict	3	1	W → R in AAH13153. Ref.7
	Sequence conflict	101	1	R → Q in AAH13153. Ref.7
	Sequence conflict	493	1	S → G in AAL27543. Ref.3
	Sequence conflict	539	1	A → T in AAL27543. Ref.3
	Sequence conflict	542	1	V → A in AAL27543. Ref.3
	Sequence conflict	703	1	Y → H in AAL27543. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q96JB6 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 13051ACADB922BBC	FASTA	756	84,483
	10 20 30 40 50 60 MAWSPPATLF LFLLLLGQPP PSRPQSLGTT KLRLVGPESK PEEGRLEVLH QGQWGTVCDD 70 80 90 100 110 120 NFAIQEATVA CRQLGFEAAL TWAHSAKYGQ GEGPIWLDNV RCVGTESSLD QCGSNGWGVS 130 140 150 160 170 180 DCSHSEDVGV ICHPRRHRGY LSETVSNALG PQGRRLEEVR LKPILASAKQ HSPVTEGAVE 190 200 210 220 230 240 VKYEGHWRQV CDQGWTMNNS RVVCGMLGFP SEVPVDSHYY RKVWDLKMRD PKSRLKSLTN 250 260 270 280 290 300 KNSFWIHQVT CLGTEPHMAN CQVQVAPARG KLRPACPGGM HAVVSCVAGP HFRPPKTKPQ 310 320 330 340 350 360 RKGSWAEEPR VRLRSGAQVG EGRVEVLMNR QWGTVCDHRW NLISASVVCR QLGFGSAREA 370 380 390 400 410 420 LFGARLGQGL GPIHLSEVRC RGYERTLSDC PALEGSQNGC QHENDAAVRC NVPNMGFQNQ 430 440 450 460 470 480 VRLAGGRIPE EGLLEVQVEV NGVPRWGSVC SENWGLTEAM VACRQLGLGF AIHAYKETWF 490 500 510 520 530 540 WSGTPRAQEV VMSGVRCSGT ELALQQCQRH GPVHCSHGGG RFLAGVSCMD SAPDLVMNAQ 550 560 570 580 590 600 LVQETAYLED RPLSQLYCAH EENCLSKSAD HMDWPYGYRR LLRFSTQIYN LGRTDFRPKT 610 620 630 640 650 660 GRDSWVWHQC HRHYHSIEVF THYDLLTLNG SKVAEGHKAS FCLEDTNCPT GLQRRYACAN 670 680 690 700 710 720 FGEQGVTVGC WDTYRHDIDC QWVDITDVGP GNYIFQVIVN PHYEVAESDF SNNMLQCRCK 730 740 750 YDGHRVWLHN CHTGNSYPAN AELSLEQEQR LRNNLI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and biological activity of a novel lysyl oxidase-related gene expressed in cartilage." Ito H., Akiyama H., Iguchi H., Iyama K., Miyamoto M., Ohsawa K., Nakamura T. J. Biol. Chem. 276:24023-24029(2001) [PubMed: 11292829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains." Maeki J.M., Tikkanen H., Kivirikko K.I. Matrix Biol. 20:493-496(2001) [PubMed: 11691589] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain." Asuncion L., Fogelgren B., Fong K.S.K., Fong S.F.T., Kim Y., Csiszar K. Matrix Biol. 20:487-491(2001) [PubMed: 11691588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-405. Tissue: Eye.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-383, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF338441 mRNA. Translation: AAK71934.1. AY036093 mRNA. Translation: AAK64186.1. AF395336 mRNA. Translation: AAL27543.1. AK025542 mRNA. Translation: BAB15167.1. AK172781 mRNA. Translation: BAD18762.1. AL139241 Genomic DNA. Translation: CAH72819.1. CH471066 Genomic DNA. Translation: EAW49886.1. BC007522 mRNA. Translation: AAH07522.1. Different initiation. BC013153 mRNA. Translation: AAH13153.1.
IPI	IPI00306402.
RefSeq	NP_115587.6. NM_032211.6.
UniGene	Hs.306814. Hs.671890.
3D structure databases
ProteinModelPortal	Q96JB6.
SMR	Q96JB6. Positions 29-136, 174-289, 306-517.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96JB6. 8 interactions.
MINT	MINT-1448374.
STRING	Q96JB6.
Polymorphism databases
DMDM	20177960.
Proteomic databases
PRIDE	Q96JB6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260702; ENSP00000260702; ENSG00000138131.
GeneID	84171.
KEGG	hsa:84171.
UCSC	uc001kpa.1. human.
Organism-specific databases
CTD	84171.
GeneCards	GC10M099997.
H-InvDB	HIX0009104.
HGNC	HGNC:17171. LOXL4.
MIM	607318. gene.
neXtProt	NX_Q96JB6.
PharmGKB	PA30431.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00590000082729.
HOGENOM	HBG717356.
HOVERGEN	HBG052336.
InParanoid	Q96JB6.
OMA	EVLHQGQ.
OrthoDB	EOG4C5CHS.
PhylomeDB	Q96JB6.
Gene expression databases
ArrayExpress	Q96JB6.
Bgee	Q96JB6.
CleanEx	HS_LOXL4.
Genevestigator	Q96JB6.
GermOnline	ENSG00000138131. Homo sapiens.
Family and domain databases
InterPro	IPR001695. Lysyl_oxidase. IPR019828. Lysyl_oxidase_CS. IPR001190. Srcr_rcpt. IPR017448. Srcr_rcpt-rel. [Graphical view]
KO	K00280.
Pfam	PF01186. Lysyl_oxidase. 1 hit. PF00530. SRCR. 4 hits. [Graphical view]
PRINTS	PR00074. LYSYLOXIDASE. PR00258. SPERACTRCPTR.
SMART	SM00202. SR. 4 hits. [Graphical view]
SUPFAM	SSF56487. Srcr_receptor. 4 hits.
PROSITE	PS00926. LYSYL_OXIDASE. 1 hit. PS00420. SRCR_1. 1 hit. PS50287. SRCR_2. 4 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	73532.
SOURCE	Search...

Entry information

Entry name

LOXL4_HUMAN

Accession

Primary (citable) accession number: Q96JB6
Secondary accession number(s): Q5W0B3 , Q96DY1, Q96PC0, Q9H6T5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.