位置:首页 > 蛋白库 > TRI46_HUMAN
TRI46_HUMAN
ID   TRI46_HUMAN             Reviewed;         759 AA.
AC   Q7Z4K8; A0AVI6; B1AVQ4; Q5VT60; Q5VT62; Q6NT17; Q6NT41; Q6ZRL7; Q9H5P2;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Tripartite motif-containing protein 46;
DE   AltName: Full=Gene Y protein;
DE            Short=GeneY;
DE   AltName: Full=Tripartite, fibronectin type-III and C-terminal SPRY motif protein;
GN   Name=TRIM46; Synonyms=TRIFIC;
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).
RX   PubMed=16434393; DOI=10.1074/jbc.m512755200;
RA   Short K.M., Cox T.C.;
RT   "Subclassification of the RBCC/TRIM superfamily reveals a novel motif
RT   necessary for microtubule binding.";
RL   J. Biol. Chem. 281:8970-8980(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5).
RC   TISSUE=Mesangial cell;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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: Microtubule-associated protein that is involved in the
CC       formation of parallel microtubule bundles linked by cross-bridges in
CC       the proximal axon. Required for the uniform orientation and maintenance
CC       of the parallel microtubule fascicles, which are important for
CC       efficient cargo delivery and trafficking in axons. Thereby also
CC       required for proper axon specification, the establishment of neuronal
CC       polarity and proper neuronal migration. {ECO:0000250|UniProtKB:Q7TNM2}.
CC   -!- SUBUNIT: Interacts with TUBB3 and TUBA4A.
CC       {ECO:0000250|UniProtKB:Q7TNM2}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q7TNM2}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q7TNM2}. Note=Microtubule-associated. Localizes
CC       to the proximal part of the axon. {ECO:0000250|UniProtKB:Q7TNM2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q7Z4K8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z4K8-2; Sequence=VSP_011983, VSP_011984;
CC       Name=3;
CC         IsoId=Q7Z4K8-3; Sequence=VSP_011980, VSP_011981, VSP_011982;
CC       Name=4;
CC         IsoId=Q7Z4K8-4; Sequence=VSP_011981, VSP_011982;
CC       Name=5;
CC         IsoId=Q7Z4K8-5; Sequence=VSP_045976;
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY251386; AAP51206.1; -; mRNA.
DR   EMBL; AK026882; BAB15580.1; -; mRNA.
DR   EMBL; AK096158; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK128139; BAC87293.1; -; mRNA.
DR   EMBL; AL607067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL713999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53120.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53123.1; -; Genomic_DNA.
DR   EMBL; BC069416; AAH69416.1; -; mRNA.
DR   EMBL; BC069568; AAH69568.1; -; mRNA.
DR   EMBL; BC126372; AAI26373.1; -; mRNA.
DR   CCDS; CCDS1097.1; -. [Q7Z4K8-1]
DR   CCDS; CCDS58033.1; -. [Q7Z4K8-5]
DR   CCDS; CCDS60285.1; -. [Q7Z4K8-2]
DR   RefSeq; NP_001243528.1; NM_001256599.1. [Q7Z4K8-5]
DR   RefSeq; NP_001243529.1; NM_001256600.1.
DR   RefSeq; NP_001243530.1; NM_001256601.1.
DR   RefSeq; NP_001269307.1; NM_001282378.1.
DR   RefSeq; NP_001269308.1; NM_001282379.1. [Q7Z4K8-2]
DR   RefSeq; NP_079334.3; NM_025058.4. [Q7Z4K8-1]
DR   AlphaFoldDB; Q7Z4K8; -.
DR   BioGRID; 123129; 24.
DR   IntAct; Q7Z4K8; 13.
DR   MINT; Q7Z4K8; -.
DR   STRING; 9606.ENSP00000334657; -.
DR   iPTMnet; Q7Z4K8; -.
DR   PhosphoSitePlus; Q7Z4K8; -.
DR   BioMuta; TRIM46; -.
DR   DMDM; 55976496; -.
DR   EPD; Q7Z4K8; -.
DR   jPOST; Q7Z4K8; -.
DR   MassIVE; Q7Z4K8; -.
DR   PaxDb; Q7Z4K8; -.
DR   PeptideAtlas; Q7Z4K8; -.
DR   PRIDE; Q7Z4K8; -.
DR   ProteomicsDB; 3355; -.
DR   ProteomicsDB; 69201; -. [Q7Z4K8-1]
DR   ProteomicsDB; 69202; -. [Q7Z4K8-2]
DR   ProteomicsDB; 69203; -. [Q7Z4K8-3]
DR   ProteomicsDB; 69204; -. [Q7Z4K8-4]
DR   Antibodypedia; 34171; 103 antibodies from 20 providers.
DR   DNASU; 80128; -.
DR   Ensembl; ENST00000334634.9; ENSP00000334657.4; ENSG00000163462.19. [Q7Z4K8-1]
DR   Ensembl; ENST00000368382.5; ENSP00000357366.1; ENSG00000163462.19. [Q7Z4K8-5]
DR   Ensembl; ENST00000368385.8; ENSP00000357369.4; ENSG00000163462.19. [Q7Z4K8-2]
DR   Ensembl; ENST00000543729.5; ENSP00000442719.2; ENSG00000163462.19. [Q7Z4K8-4]
DR   GeneID; 80128; -.
DR   KEGG; hsa:80128; -.
DR   MANE-Select; ENST00000334634.9; ENSP00000334657.4; NM_025058.5; NP_079334.3.
DR   UCSC; uc001fhr.6; human. [Q7Z4K8-1]
DR   CTD; 80128; -.
DR   DisGeNET; 80128; -.
DR   GeneCards; TRIM46; -.
DR   HGNC; HGNC:19019; TRIM46.
DR   HPA; ENSG00000163462; Tissue enhanced (brain).
DR   MIM; 600986; gene.
DR   neXtProt; NX_Q7Z4K8; -.
DR   OpenTargets; ENSG00000163462; -.
DR   PharmGKB; PA134914315; -.
DR   VEuPathDB; HostDB:ENSG00000163462; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000158021; -.
DR   HOGENOM; CLU_013137_19_2_1; -.
DR   InParanoid; Q7Z4K8; -.
DR   OMA; AEMDFKT; -.
DR   OrthoDB; 180330at2759; -.
DR   PhylomeDB; Q7Z4K8; -.
DR   TreeFam; TF315216; -.
DR   PathwayCommons; Q7Z4K8; -.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   SignaLink; Q7Z4K8; -.
DR   BioGRID-ORCS; 80128; 23 hits in 1109 CRISPR screens.
DR   ChiTaRS; TRIM46; human.
DR   GenomeRNAi; 80128; -.
DR   Pharos; Q7Z4K8; Tbio.
DR   PRO; PR:Q7Z4K8; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q7Z4K8; protein.
DR   Bgee; ENSG00000163462; Expressed in cortical plate and 119 other tissues.
DR   ExpressionAtlas; Q7Z4K8; baseline and differential.
DR   Genevisible; Q7Z4K8; HS.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0043194; C:axon initial segment; IEA:Ensembl.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0044304; C:main axon; ISS:ARUK-UCL.
DR   GO; GO:1990769; C:proximal neuron projection; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048490; P:anterograde synaptic vesicle transport; IBA:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR   GO; GO:0001578; P:microtubule bundle formation; IBA:GO_Central.
DR   GO; GO:0030517; P:negative regulation of axon extension; ISS:ARUK-UCL.
DR   GO; GO:0001764; P:neuron migration; IBA:GO_Central.
DR   GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; ISS:ARUK-UCL.
DR   GO; GO:0099612; P:protein localization to axon; IEA:Ensembl.
DR   GO; GO:0032880; P:regulation of protein localization; ISS:ARUK-UCL.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd12895; SPRY_PRY_TRIM46; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR040859; Midline-1_COS.
DR   InterPro; IPR035731; SPRY/PRY_TRIM46.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF18568; COS; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..759
FT                   /note="Tripartite motif-containing protein 46"
FT                   /id="PRO_0000056268"
FT   DOMAIN          370..427
FT                   /note="COS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT   DOMAIN          429..528
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          526..747
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         33..59
FT                   /note="RING-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         172..231
FT                   /note="RING-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         222..263
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          1..166
FT                   /note="Required for proximal axon localization, axon
FT                   formation and migration"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TNM2"
FT   REGION          67..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..429
FT                   /note="Required for microtubule association, proximal axon
FT                   localization and axon formation"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TNM2"
FT   REGION          623..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          322..400
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        75..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         255
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TNM2"
FT   MOD_RES         627
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TNM2"
FT   VAR_SEQ         1..23
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045976"
FT   VAR_SEQ         1..21
FT                   /note="MAEGEDMQTFTSIMDALVRIS -> MERAGWSANLAWLSGGITLCSGEREAR
FT                   DRGLGRSVNQPKAGALEKLQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_011980"
FT   VAR_SEQ         429..498
FT                   /note="VPEAPVIDTQRTFAYDQIFLCWRLPPHSPPAWHYTVEFRRTDVPAQPGPTRW
FT                   QRREEVRGTSALLENPDT -> GCGHRGLCSGAPQCLRPPSLTPSAPLPMIRSSCAGGC
FT                   PPIHHLPGTIPLSSGARMCLLSQAPPAGSGGRR (in isoform 3 and isoform
FT                   4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011981"
FT   VAR_SEQ         499..759
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011982"
FT   VAR_SEQ         530..551
FT                   /note="VLHFFLDSRWGASRERLAISKD -> GIQNLARRGGACLQFQLLGRLR (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_011983"
FT   VAR_SEQ         552..759
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_011984"
FT   CONFLICT        18
FT                   /note="V -> A (in Ref. 5; AAH69568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="R -> H (in Ref. 1; AAP51206 and 2; BAB15580)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="T -> A (in Ref. 1; AAP51206 and 2; BAB15580)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="P -> R (in Ref. 5; AAH69568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        406
FT                   /note="S -> P (in Ref. 2; AK096158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        414
FT                   /note="V -> A (in Ref. 2; AK096158)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   759 AA;  83424 MW;  FEA9DDE1434EB7AA CRC64;
     MAEGEDMQTF TSIMDALVRI STSMKNMEKE LLCPVCQEMY KQPLVLPCTH NVCQACAREV
     LGQQGYIGHG GDPSSEPTSP ASTPSTRSPR LSRRTLPKPD RLDRLLKSGF GTYPGRKRGA
     LHPQVIMFPC PACQGDVELG ERGLAGLFRN LTLERVVERY RQSVSVGGAI LCQLCKPPPL
     EATKGCTECR ATFCNECFKL FHPWGTQKAQ HEPTLPTLSF RPKGLMCPDH KEEVTHYCKT
     CQRLVCQLCR VRRTHSGHKI TPVLSAYQAL KDKLTKSLTY ILGNQDTVQT QICELEEAVR
     HTEVSGQQAK EEVSQLVRGL GAVLEEKRAS LLQAIEECQQ ERLARLSAQI QEHRSLLDGS
     GLVGYAQEVL KETDQPCFVQ AAKQLHNRIA RATEALQTFR PAASSSFRHC QLDVGREMKL
     LTELNFLRVP EAPVIDTQRT FAYDQIFLCW RLPPHSPPAW HYTVEFRRTD VPAQPGPTRW
     QRREEVRGTS ALLENPDTGS VYVLRVRGCN KAGYGEYSED VHLHTPPAPV LHFFLDSRWG
     ASRERLAISK DQRAVRSVPG LPLLLAADRL LTGCHLSVDV VLGDVAVTQG RSYWACAVDP
     ASYLVKVGVG LESKLQESFQ GAPDVISPRY DPDSGHDSGA EDATVEASPP FAFLTIGMGK
     ILLGSGASSN AGLTGRDGPT AGCTVPLPPR LGICLDYERG RVSFLDAVSF RGLLECPLDC
     SGPVCPAFCF IGGGAVQLQE PVGTKPERKV TIGGFAKLD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024