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LOXL4_HUMAN
ID   LOXL4_HUMAN             Reviewed;         756 AA.
AC   Q96JB6; Q5W0B3; Q96DY1; Q96PC0; Q9H6T5;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Lysyl oxidase homolog 4;
DE            EC=1.4.3.-;
DE   AltName: Full=Lysyl oxidase-like protein 4;
DE   AltName: Full=Lysyl oxidase-related protein C;
DE   Flags: Precursor;
GN   Name=LOXL4; Synonyms=LOXC;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=11292829; DOI=10.1074/jbc.m100861200;
RA   Ito H., Akiyama H., Iguchi H., Iyama K., Miyamoto M., Ohsawa K.,
RA   Nakamura T.;
RT   "Molecular cloning and biological activity of a novel lysyl oxidase-related
RT   gene expressed in cartilage.";
RL   J. Biol. Chem. 276:24023-24029(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11691589; DOI=10.1016/s0945-053x(01)00157-3;
RA   Maeki J.M., Tikkanen H., Kivirikko K.I.;
RT   "Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the
RT   third member of the lysyl oxidase-related subfamily with four scavenger
RT   receptor cysteine-rich domains.";
RL   Matrix Biol. 20:493-496(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=11691588; DOI=10.1016/s0945-053x(01)00161-5;
RA   Asuncion L., Fogelgren B., Fong K.S.K., Fong S.F.T., Kim Y., Csiszar K.;
RT   "A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an
RT   altered scavenger receptor cysteine rich domain.";
RL   Matrix Biol. 20:487-491(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-405.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
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   -!- FUNCTION: May modulate the formation of a collagenous extracellular
CC       matrix.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P16636};
CC   -!- COFACTOR:
CC       Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489;
CC         Evidence={ECO:0000250|UniProtKB:P33072};
CC       Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072};
CC   -!- INTERACTION:
CC       Q96JB6; Q86V38: ATN1; NbExp=3; IntAct=EBI-749562, EBI-11954292;
CC       Q96JB6; P55212: CASP6; NbExp=3; IntAct=EBI-749562, EBI-718729;
CC       Q96JB6; P02489: CRYAA; NbExp=3; IntAct=EBI-749562, EBI-6875961;
CC       Q96JB6; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-749562, EBI-12593112;
CC       Q96JB6; P22607: FGFR3; NbExp=3; IntAct=EBI-749562, EBI-348399;
CC       Q96JB6; Q14957: GRIN2C; NbExp=3; IntAct=EBI-749562, EBI-8285963;
CC       Q96JB6; P28799: GRN; NbExp=3; IntAct=EBI-749562, EBI-747754;
CC       Q96JB6; P06396: GSN; NbExp=3; IntAct=EBI-749562, EBI-351506;
CC       Q96JB6; P04792: HSPB1; NbExp=3; IntAct=EBI-749562, EBI-352682;
CC       Q96JB6; O60341: KDM1A; NbExp=2; IntAct=EBI-749562, EBI-710124;
CC       Q96JB6; O60333-2: KIF1B; NbExp=3; IntAct=EBI-749562, EBI-10975473;
CC       Q96JB6; O14901: KLF11; NbExp=3; IntAct=EBI-749562, EBI-948266;
CC       Q96JB6; Q92876: KLK6; NbExp=3; IntAct=EBI-749562, EBI-2432309;
CC       Q96JB6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-749562, EBI-21591415;
CC       Q96JB6; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-749562, EBI-912440;
CC       Q96JB6; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-749562, EBI-396669;
CC       Q96JB6; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-749562, EBI-5235340;
CC       Q96JB6; Q15645: TRIP13; NbExp=6; IntAct=EBI-749562, EBI-358993;
CC       Q96JB6; O76024: WFS1; NbExp=3; IntAct=EBI-749562, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in many tissues, the highest levels among
CC       the tissues studied being in the skeletal muscle, testis and pancreas.
CC       Expressed in cartilage.
CC   -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by
CC       condensation of the epsilon-amino group of a lysine with a topaquinone
CC       produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}.
CC   -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH07522.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/LOXL4ID41193ch10q24.html";
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DR   EMBL; AF338441; AAK71934.1; -; mRNA.
DR   EMBL; AY036093; AAK64186.1; -; mRNA.
DR   EMBL; AF395336; AAL27543.1; -; mRNA.
DR   EMBL; AK025542; BAB15167.1; -; mRNA.
DR   EMBL; AK172781; BAD18762.1; -; mRNA.
DR   EMBL; AL139241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW49886.1; -; Genomic_DNA.
DR   EMBL; BC007522; AAH07522.1; ALT_INIT; mRNA.
DR   EMBL; BC013153; AAH13153.1; -; mRNA.
DR   CCDS; CCDS7473.1; -.
DR   RefSeq; NP_115587.6; NM_032211.6.
DR   AlphaFoldDB; Q96JB6; -.
DR   SMR; Q96JB6; -.
DR   BioGRID; 123925; 121.
DR   IntAct; Q96JB6; 32.
DR   MINT; Q96JB6; -.
DR   STRING; 9606.ENSP00000260702; -.
DR   BindingDB; Q96JB6; -.
DR   ChEMBL; CHEMBL4295926; -.
DR   GlyConnect; 1482; 1 N-Linked glycan (1 site).
DR   GlyGen; Q96JB6; 2 sites.
DR   iPTMnet; Q96JB6; -.
DR   PhosphoSitePlus; Q96JB6; -.
DR   BioMuta; LOXL4; -.
DR   DMDM; 20177960; -.
DR   EPD; Q96JB6; -.
DR   jPOST; Q96JB6; -.
DR   MassIVE; Q96JB6; -.
DR   MaxQB; Q96JB6; -.
DR   PaxDb; Q96JB6; -.
DR   PeptideAtlas; Q96JB6; -.
DR   PRIDE; Q96JB6; -.
DR   ProteomicsDB; 76933; -.
DR   Antibodypedia; 31028; 225 antibodies from 23 providers.
DR   DNASU; 84171; -.
DR   Ensembl; ENST00000260702.4; ENSP00000260702.3; ENSG00000138131.4.
DR   GeneID; 84171; -.
DR   KEGG; hsa:84171; -.
DR   MANE-Select; ENST00000260702.4; ENSP00000260702.3; NM_032211.7; NP_115587.6.
DR   UCSC; uc001kpa.2; human.
DR   CTD; 84171; -.
DR   DisGeNET; 84171; -.
DR   GeneCards; LOXL4; -.
DR   HGNC; HGNC:17171; LOXL4.
DR   HPA; ENSG00000138131; Low tissue specificity.
DR   MIM; 607318; gene.
DR   neXtProt; NX_Q96JB6; -.
DR   OpenTargets; ENSG00000138131; -.
DR   PharmGKB; PA30431; -.
DR   VEuPathDB; HostDB:ENSG00000138131; -.
DR   eggNOG; ENOG502QSX8; Eukaryota.
DR   GeneTree; ENSGT00940000157042; -.
DR   HOGENOM; CLU_002555_3_0_1; -.
DR   InParanoid; Q96JB6; -.
DR   OMA; GMQRRYA; -.
DR   OrthoDB; 815466at2759; -.
DR   PhylomeDB; Q96JB6; -.
DR   TreeFam; TF326061; -.
DR   PathwayCommons; Q96JB6; -.
DR   Reactome; R-HSA-1566948; Elastic fibre formation.
DR   Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR   SignaLink; Q96JB6; -.
DR   BioGRID-ORCS; 84171; 9 hits in 1065 CRISPR screens.
DR   ChiTaRS; LOXL4; human.
DR   GeneWiki; LOXL4; -.
DR   GenomeRNAi; 84171; -.
DR   Pharos; Q96JB6; Tchem.
DR   PRO; PR:Q96JB6; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q96JB6; protein.
DR   Bgee; ENSG00000138131; Expressed in tibia and 139 other tissues.
DR   Genevisible; Q96JB6; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004720; F:protein-lysine 6-oxidase activity; IBA:GO_Central.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR   GO; GO:0018057; P:peptidyl-lysine oxidation; IBA:GO_Central.
DR   Gene3D; 3.10.250.10; -; 4.
DR   InterPro; IPR001695; Lysyl_oxidase.
DR   InterPro; IPR019828; Lysyl_oxidase_CS.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   Pfam; PF01186; Lysyl_oxidase; 1.
DR   Pfam; PF00530; SRCR; 4.
DR   PRINTS; PR00074; LYSYLOXIDASE.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00202; SR; 4.
DR   SUPFAM; SSF56487; SSF56487; 4.
DR   PROSITE; PS00926; LYSYL_OXIDASE; 1.
DR   PROSITE; PS00420; SRCR_1; 1.
DR   PROSITE; PS50287; SRCR_2; 4.
PE   1: Evidence at protein level;
KW   Copper; Disulfide bond; Glycoprotein; LTQ; Metal-binding; Oxidoreductase;
KW   Reference proteome; Repeat; Secreted; Signal; TPQ.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..756
FT                   /note="Lysyl oxidase homolog 4"
FT                   /id="PRO_0000018535"
FT   DOMAIN          32..133
FT                   /note="SRCR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DOMAIN          159..287
FT                   /note="SRCR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DOMAIN          311..411
FT                   /note="SRCR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DOMAIN          421..529
FT                   /note="SRCR 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   REGION          533..736
FT                   /note="Lysyl-oxidase like"
FT   BINDING         611
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255"
FT   BINDING         613
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255"
FT   BINDING         615
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         674
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P33072"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        629
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        58..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        71..132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        102..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        191..276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        204..286
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        251..261
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        336..400
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        349..410
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        380..390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        450..515
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        463..528
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        497..507
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        558..564
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        610..658
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        642..648
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        670..680
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        717..731
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   CROSSLNK        638..674
FT                   /note="Lysine tyrosylquinone (Lys-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P33072"
FT   VARIANT         154
FT                   /note="R -> Q (in dbSNP:rs33995374)"
FT                   /id="VAR_050012"
FT   VARIANT         372
FT                   /note="P -> T (in dbSNP:rs11189525)"
FT                   /id="VAR_059431"
FT   VARIANT         405
FT                   /note="D -> A (in dbSNP:rs1983864)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_050013"
FT   CONFLICT        3
FT                   /note="W -> R (in Ref. 7; AAH13153)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="R -> Q (in Ref. 7; AAH13153)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        493
FT                   /note="S -> G (in Ref. 3; AAL27543)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        539
FT                   /note="A -> T (in Ref. 3; AAL27543)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        542
FT                   /note="V -> A (in Ref. 3; AAL27543)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        703
FT                   /note="Y -> H (in Ref. 3; AAL27543)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   756 AA;  84483 MW;  13051ACADB922BBC CRC64;
     MAWSPPATLF LFLLLLGQPP PSRPQSLGTT KLRLVGPESK PEEGRLEVLH QGQWGTVCDD
     NFAIQEATVA CRQLGFEAAL TWAHSAKYGQ GEGPIWLDNV RCVGTESSLD QCGSNGWGVS
     DCSHSEDVGV ICHPRRHRGY LSETVSNALG PQGRRLEEVR LKPILASAKQ HSPVTEGAVE
     VKYEGHWRQV CDQGWTMNNS RVVCGMLGFP SEVPVDSHYY RKVWDLKMRD PKSRLKSLTN
     KNSFWIHQVT CLGTEPHMAN CQVQVAPARG KLRPACPGGM HAVVSCVAGP HFRPPKTKPQ
     RKGSWAEEPR VRLRSGAQVG EGRVEVLMNR QWGTVCDHRW NLISASVVCR QLGFGSAREA
     LFGARLGQGL GPIHLSEVRC RGYERTLSDC PALEGSQNGC QHENDAAVRC NVPNMGFQNQ
     VRLAGGRIPE EGLLEVQVEV NGVPRWGSVC SENWGLTEAM VACRQLGLGF AIHAYKETWF
     WSGTPRAQEV VMSGVRCSGT ELALQQCQRH GPVHCSHGGG RFLAGVSCMD SAPDLVMNAQ
     LVQETAYLED RPLSQLYCAH EENCLSKSAD HMDWPYGYRR LLRFSTQIYN LGRTDFRPKT
     GRDSWVWHQC HRHYHSIEVF THYDLLTLNG SKVAEGHKAS FCLEDTNCPT GLQRRYACAN
     FGEQGVTVGC WDTYRHDIDC QWVDITDVGP GNYIFQVIVN PHYEVAESDF SNNMLQCRCK
     YDGHRVWLHN CHTGNSYPAN AELSLEQEQR LRNNLI
 
 
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