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LY6H_HUMAN
ID   LY6H_HUMAN              Reviewed;         140 AA.
AC   O94772; B2RAD2; J3KQI0; Q6IAX0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Lymphocyte antigen 6H;
DE            Short=Ly-6H;
DE   Flags: Precursor;
GN   Name=LY6H;
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] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=9799603; DOI=10.1006/geno.1998.5462;
RA   Horie M., Okutomi K., Taniguchi Y., Ohbuchi Y., Suzuki M., Takahashi E.;
RT   "Isolation and characterization of a new member of the human Ly6 gene
RT   family (LY6H).";
RL   Genomics 53:365-368(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
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] (ISOFORM 1).
RC   TISSUE=Brain;
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: Believed to act as a modulator of nicotinic acetylcholine
CC       receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-
CC       containing nAChRs maximum response. May play a role in the
CC       intracellular trafficking of alpha-7-containing nAChRs and may inhibit
CC       their expression at the cell surface. Seems to inhibit alpha-7/CHRNA7
CC       signaling in hippocampal neurons. {ECO:0000250|UniProtKB:F1LNW6,
CC       ECO:0000250|UniProtKB:Q9WUC3}.
CC   -!- SUBUNIT: Interacts with CHRNA4 and CHRNA7.
CC       {ECO:0000250|UniProtKB:Q9WUC3}.
CC   -!- INTERACTION:
CC       O94772; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-724687, EBI-3958099;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O94772-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O94772-2; Sequence=VSP_053497;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain (cerebral cortex,
CC       amygdala, hippocampus and subthalamic nucleus) and in acute human
CC       leukemic cell line MOLT-3. Also found in lower levels in testis,
CC       pancreas, small intestine and colon.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AB012293; BAA34115.1; -; mRNA.
DR   EMBL; BX419752; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CR457034; CAG33315.1; -; mRNA.
DR   EMBL; AK314139; BAG36829.1; -; mRNA.
DR   EMBL; AC083982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471162; EAW82277.1; -; Genomic_DNA.
DR   EMBL; BC028894; AAH28894.1; -; mRNA.
DR   EMBL; BC030192; AAH30192.1; -; mRNA.
DR   CCDS; CCDS47926.1; -. [O94772-2]
DR   CCDS; CCDS6396.1; -. [O94772-1]
DR   RefSeq; NP_001123950.1; NM_001130478.1. [O94772-2]
DR   RefSeq; NP_001129127.1; NM_001135655.1. [O94772-2]
DR   RefSeq; NP_002338.3; NM_002347.4. [O94772-1]
DR   RefSeq; XP_016868903.1; XM_017013414.1.
DR   AlphaFoldDB; O94772; -.
DR   BioGRID; 110240; 70.
DR   IntAct; O94772; 3.
DR   STRING; 9606.ENSP00000399485; -.
DR   GlyGen; O94772; 1 site.
DR   iPTMnet; O94772; -.
DR   PhosphoSitePlus; O94772; -.
DR   BioMuta; LY6H; -.
DR   jPOST; O94772; -.
DR   MassIVE; O94772; -.
DR   PaxDb; O94772; -.
DR   PeptideAtlas; O94772; -.
DR   PRIDE; O94772; -.
DR   ProteomicsDB; 50435; -. [O94772-1]
DR   Antibodypedia; 27844; 74 antibodies from 16 providers.
DR   DNASU; 4062; -.
DR   Ensembl; ENST00000342752.9; ENSP00000342711.4; ENSG00000176956.13. [O94772-2]
DR   Ensembl; ENST00000414417.6; ENSP00000399485.2; ENSG00000176956.13. [O94772-2]
DR   Ensembl; ENST00000430474.6; ENSP00000409899.2; ENSG00000176956.13. [O94772-1]
DR   Ensembl; ENST00000610554.2; ENSP00000478470.1; ENSG00000274488.4. [O94772-1]
DR   Ensembl; ENST00000615409.1; ENSP00000480084.1; ENSG00000176956.13. [O94772-1]
DR   Ensembl; ENST00000615434.4; ENSP00000482094.2; ENSG00000274488.4. [O94772-2]
DR   Ensembl; ENST00000631670.1; ENSP00000487965.1; ENSG00000274488.4. [O94772-2]
DR   GeneID; 4062; -.
DR   KEGG; hsa:4062; -.
DR   MANE-Select; ENST00000342752.9; ENSP00000342711.4; NM_001135655.2; NP_001129127.1. [O94772-2]
DR   UCSC; uc011lka.2; human. [O94772-1]
DR   CTD; 4062; -.
DR   DisGeNET; 4062; -.
DR   GeneCards; LY6H; -.
DR   HGNC; HGNC:6728; LY6H.
DR   HPA; ENSG00000176956; Tissue enhanced (brain, pituitary gland).
DR   MIM; 603625; gene.
DR   neXtProt; NX_O94772; -.
DR   OpenTargets; ENSG00000176956; -.
DR   PharmGKB; PA30492; -.
DR   VEuPathDB; HostDB:ENSG00000176956; -.
DR   eggNOG; ENOG502RVP9; Eukaryota.
DR   GeneTree; ENSGT00940000154560; -.
DR   HOGENOM; CLU_106772_1_1_1; -.
DR   InParanoid; O94772; -.
DR   OMA; DVECCEK; -.
DR   OrthoDB; 1482771at2759; -.
DR   PhylomeDB; O94772; -.
DR   TreeFam; TF337757; -.
DR   PathwayCommons; O94772; -.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   SignaLink; O94772; -.
DR   BioGRID-ORCS; 4062; 6 hits in 1066 CRISPR screens.
DR   GenomeRNAi; 4062; -.
DR   Pharos; O94772; Tbio.
DR   PRO; PR:O94772; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; O94772; protein.
DR   Bgee; ENSG00000176956; Expressed in Ammon's horn and 90 other tissues.
DR   Genevisible; O94772; HS.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0033130; F:acetylcholine receptor binding; IBA:GO_Central.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IBA:GO_Central.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   CDD; cd00117; LU; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   Pfam; PF00021; UPAR_LY6; 1.
DR   SMART; SM00134; LU; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..115
FT                   /note="Lymphocyte antigen 6H"
FT                   /id="PRO_0000036148"
FT   PROPEP          116..140
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036149"
FT   DOMAIN          26..91
FT                   /note="UPAR/Ly6"
FT   LIPID           115
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..52
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
FT   DISULFID        31..40
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
FT   DISULFID        45..73
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
FT   DISULFID        77..104
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
FT   DISULFID        105..110
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
FT   VAR_SEQ         1
FT                   /note="M -> MLAPQRTRAPSPRAAPRPTRSM (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_053497"
FT   CONFLICT        4
FT                   /note="A -> T (in Ref. 3; CAG33315)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  14669 MW;  A9274BFE89B6CBA3 CRC64;
     MLPAAMKGLG LALLAVLLCS APAHGLWCQD CTLTTNSSHC TPKQCQPSDT VCASVRITDP
     SSSRKDHSVN KMCASSCDFV KRHFFSDYLM GFINSGILKV DVDCCEKDLC NGAAGAGHSP
     WALAGGLLLS LGPALLWAGP
 
 
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