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 24-JAN-2024, entry version 178.
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}.
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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 SMR; Q7Z4K8; -.
DR BioGRID; 123129; 28.
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; 9606-ENSP00000334657; -.
DR PeptideAtlas; 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; 119 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 AGR; HGNC:19019; -.
DR CTD; 80128; -.
DR DisGeNET; 80128; -.
DR GeneCards; TRIM46; -.
DR HGNC; HGNC:19019; TRIM46.
DR HPA; ENSG00000163462; Tissue enriched (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; XIARATE; -.
DR OrthoDB; 5383069at2759; -.
DR PhylomeDB; Q7Z4K8; -.
DR TreeFam; TF315216; -.
DR PathwayCommons; Q7Z4K8; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q7Z4K8; -.
DR SIGNOR; Q7Z4K8; -.
DR BioGRID-ORCS; 80128; 33 hits in 1186 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 120 other cell types or 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; cd19849; Bbox1_TRIM46_C-I; 1.
DR CDD; cd19786; Bbox2_TRIM46_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16757; RING-HC_TRIM46_C-I; 1.
DR CDD; cd12895; SPRY_PRY_TRIM46; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR027370; Znf-RING_euk.
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 PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR PANTHER; PTHR24099:SF20; TRIPARTITE MOTIF-CONTAINING PROTEIN 46; 1.
DR Pfam; PF18568; COS; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57850; RING/U-box; 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
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