ID   Q5PR71_MOUSE            Unreviewed;       393 AA.
AC   Q5PR71;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   02-SEP-2026, entry version 85.
DE   RecName: Full=Lysyl oxidase homolog 2 {ECO:0000256|ARBA:ARBA00039813};
DE   AltName: Full=Lysyl oxidase-like protein 2 {ECO:0000256|ARBA:ARBA00042423};
GN   Name=Loxl2 {ECO:0000313|EMBL:AAH86801.1, ECO:0000313|MGI:MGI:2137913};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH86801.1};
RN   [1] {ECO:0000313|EMBL:AAH86801.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH86801.1};
RC   TISSUE=Eye {ECO:0000313|EMBL:AAH86801.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Component of some chromatin repressor complex. Interacts with
CC       SNAI1. Interacts with TAF10. Interacts with HSPA5. Interacts with
CC       EFEMP2. {ECO:0000256|ARBA:ARBA00046895}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   EMBL; BC086801; AAH86801.1; -; mRNA.
DR   AlphaFoldDB; Q5PR71; -.
DR   PeptideAtlas; Q5PR71; -.
DR   AGR; MGI:2137913; -.
DR   MGI; MGI:2137913; Loxl2.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   FunFam; 3.10.250.10:FF:000001; Lysyl oxidase 4 isoform X1; 2.
DR   FunFam; 3.10.250.10:FF:000014; Lysyl oxidase homolog 2; 1.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 3.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   PANTHER; PTHR45817:SF1; LYSYL OXIDASE HOMOLOG 2; 1.
DR   PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1.
DR   Pfam; PF00530; SRCR; 3.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00202; SR; 3.
DR   SUPFAM; SSF56487; SRCR-like; 3.
DR   PROSITE; PS00420; SRCR_1; 1.
DR   PROSITE; PS50287; SRCR_2; 3.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00196}; Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..393
FT                   /note="Lysyl oxidase homolog 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004261339"
FT   DOMAIN          61..162
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          191..305
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          329..393
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DISULFID        87..151
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        100..161
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        131..141
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        268..278
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ   SEQUENCE   393 AA;  43862 MW;  D45E5CA31DC34DB7 CRC64;
     MELHFGSCLS GCLALLVLLP SLSLAQYEGW PYQLQYPEYF QQPAPEHHQR QVPSDVVKIQ
     VRLAGQKRKH NEGRVEVYYE GQWGTVCDDD FSIHAAHVVC RQVGYVEAKS WAASSSYGPG
     EGPIWLDNIY CTGKESTLAS CSSNGWGVTD CKHTEDVGVV CSEKRIPGFK FDNSLINQIE
     SLNIQVEDIR IRPILSAFRH RKPVTEGYVE VKEGKAWKQI CNKHWTAKNS HVVCGMFGFP
     AEKTYNPKAY KTFASRRKLR YWKFSMNCTG TEAHISSCKL GPSVTRDPVK NATCENGQPA
     VVSCVPSQIF SPDGPSRFRK AYKPEQPLVR LRGGAQVGEG RVEVLKNGEW GTICDDKWDL
     VSASVVCREL GFGTAKEAIT GSRLGQGMAE WRC
//