RN170_HUMAN
ID RN170_HUMAN Reviewed; 258 AA.
AC Q96K19; D3DSY6; E9PIL4; Q7Z483; Q86YC0; Q8IXR7; Q8N2B5; Q8N5G9; Q8NG30;
AC Q9H0V6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=E3 ubiquitin-protein ligase RNF170;
DE EC=2.3.2.27;
DE AltName: Full=Putative LAG1-interacting protein;
DE AltName: Full=RING finger protein 170;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF170 {ECO:0000305};
GN Name=RNF170;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Amygdala, and Placenta;
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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 5 AND 6).
RC TISSUE=Brain, Lung, Pancreas, and Placenta;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-258 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Pan H., Xu Z.G., Huo K.K., Li Y.Y.;
RT "Interactors of a human homolog of yeast LAG1 gene.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH
RP ERLIN1/ERLIN2 COMPLEX AND ITPR1.
RX PubMed=21610068; DOI=10.1074/jbc.m111.251983;
RA Lu J.P., Wang Y., Sliter D.A., Pearce M.M., Wojcikiewicz R.J.;
RT "RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase,
RT mediates inositol 1,4,5-trisphosphate receptor ubiquitination and
RT degradation.";
RL J. Biol. Chem. 286:24426-24433(2011).
RN [9]
RP VARIANT SNAX1 CYS-199, AND TISSUE SPECIFICITY.
RX PubMed=21115467; DOI=10.1093/brain/awq329;
RA Valdmanis P.N., Dupre N., Lachance M., Stochmanski S.J., Belzil V.V.,
RA Dion P.A., Thiffault I., Brais B., Weston L., Saint-Amant L., Samuels M.E.,
RA Rouleau G.A.;
RT "A mutation in the RNF170 gene causes autosomal dominant sensory ataxia.";
RL Brain 134:602-607(2011).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays an essential role in
CC stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1)
CC ubiquitination and degradation via the endoplasmic reticulum-associated
CC degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting
CC cells. {ECO:0000269|PubMed:21610068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Constitutively associated with the ERLIN1/ERLIN 2 complex.
CC Interacts with activated ITPR1. {ECO:0000269|PubMed:21610068}.
CC -!- INTERACTION:
CC Q96K19; P60900: PSMA6; NbExp=3; IntAct=EBI-2130336, EBI-357793;
CC Q96K19-5; Q96LL9: DNAJC30; NbExp=3; IntAct=EBI-12055631, EBI-8639143;
CC Q96K19-5; B0YJ81: HACD1; NbExp=3; IntAct=EBI-12055631, EBI-12051643;
CC Q96K19-5; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-12055631, EBI-11721828;
CC Q96K19-5; O43765: SGTA; NbExp=3; IntAct=EBI-12055631, EBI-347996;
CC Q96K19-5; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-12055631, EBI-744081;
CC Q96K19-5; Q8TB61: SLC35B2; NbExp=3; IntAct=EBI-12055631, EBI-1054782;
CC Q96K19-5; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-12055631, EBI-10244848;
CC Q96K19-5; Q14849: STARD3; NbExp=3; IntAct=EBI-12055631, EBI-9819324;
CC Q96K19-5; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-12055631, EBI-1057733;
CC Q96K19-5; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12055631, EBI-12111910;
CC Q96K19-5; O00526: UPK2; NbExp=3; IntAct=EBI-12055631, EBI-10179682;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21610068}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21610068}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q96K19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96K19-2; Sequence=VSP_023856;
CC Name=3;
CC IsoId=Q96K19-3; Sequence=VSP_023855, VSP_023857;
CC Name=4;
CC IsoId=Q96K19-4; Sequence=VSP_023851, VSP_023852;
CC Name=5;
CC IsoId=Q96K19-5; Sequence=VSP_023853, VSP_023854;
CC Name=6;
CC IsoId=Q96K19-6; Sequence=VSP_044556;
CC -!- TISSUE SPECIFICITY: Expressed in the spinal chord.
CC {ECO:0000269|PubMed:21115467}.
CC -!- DISEASE: Ataxia, sensory, 1, autosomal dominant (SNAX1) [MIM:608984]: A
CC rare disease characterized by progressive ataxia caused by degeneration
CC of the posterior columns of the spinal cord. Affected individuals have
CC a reduced ability to feel pain, temperature and vibration, particularly
CC in the hands and feet. Their most prominent feature is an ataxic gait
CC resulting from a severe loss of proprioception. Thus, patients rely on
CC visual cues for maintaining proper body posture, such that they are
CC unable to remain upright if their eyes are closed (Romberg sign).
CC {ECO:0000269|PubMed:21115467}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39461.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH44566.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK027748; BAB55340.1; -; mRNA.
DR EMBL; AK090864; BAC03534.1; -; mRNA.
DR EMBL; AC009634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63201.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63203.1; -; Genomic_DNA.
DR EMBL; BC013422; AAH13422.1; -; mRNA.
DR EMBL; BC032393; AAH32393.1; -; mRNA.
DR EMBL; BC039461; AAH39461.1; ALT_INIT; mRNA.
DR EMBL; BC044566; AAH44566.1; ALT_INIT; mRNA.
DR EMBL; BC058289; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL136620; CAB66555.1; -; mRNA.
DR EMBL; AF209504; AAM92891.1; -; mRNA.
DR CCDS; CCDS55229.1; -. [Q96K19-6]
DR CCDS; CCDS55230.1; -. [Q96K19-3]
DR CCDS; CCDS6138.1; -. [Q96K19-1]
DR RefSeq; NP_001153695.1; NM_001160223.1. [Q96K19-1]
DR RefSeq; NP_001153696.1; NM_001160224.1. [Q96K19-3]
DR RefSeq; NP_001153697.1; NM_001160225.1. [Q96K19-6]
DR RefSeq; NP_112216.3; NM_030954.3. [Q96K19-1]
DR RefSeq; XP_006716467.1; XM_006716404.2. [Q96K19-1]
DR RefSeq; XP_011542968.1; XM_011544666.2. [Q96K19-1]
DR RefSeq; XP_016869370.1; XM_017013881.1. [Q96K19-1]
DR RefSeq; XP_016869371.1; XM_017013882.1. [Q96K19-6]
DR AlphaFoldDB; Q96K19; -.
DR SMR; Q96K19; -.
DR BioGRID; 123583; 73.
DR CORUM; Q96K19; -.
DR IntAct; Q96K19; 41.
DR MINT; Q96K19; -.
DR STRING; 9606.ENSP00000445725; -.
DR iPTMnet; Q96K19; -.
DR PhosphoSitePlus; Q96K19; -.
DR BioMuta; RNF170; -.
DR DMDM; 134035027; -.
DR EPD; Q96K19; -.
DR jPOST; Q96K19; -.
DR MassIVE; Q96K19; -.
DR MaxQB; Q96K19; -.
DR PaxDb; Q96K19; -.
DR PeptideAtlas; Q96K19; -.
DR PRIDE; Q96K19; -.
DR ProteomicsDB; 20847; -.
DR ProteomicsDB; 77025; -. [Q96K19-1]
DR ProteomicsDB; 77026; -. [Q96K19-2]
DR ProteomicsDB; 77027; -. [Q96K19-3]
DR ProteomicsDB; 77028; -. [Q96K19-4]
DR ProteomicsDB; 77029; -. [Q96K19-5]
DR Antibodypedia; 24165; 123 antibodies from 24 providers.
DR DNASU; 81790; -.
DR Ensembl; ENST00000240159.8; ENSP00000240159.4; ENSG00000120925.16. [Q96K19-5]
DR Ensembl; ENST00000319073.5; ENSP00000325969.5; ENSG00000120925.16. [Q96K19-5]
DR Ensembl; ENST00000319104.7; ENSP00000326138.3; ENSG00000120925.16. [Q96K19-3]
DR Ensembl; ENST00000526349.5; ENSP00000435782.1; ENSG00000120925.16. [Q96K19-6]
DR Ensembl; ENST00000527424.6; ENSP00000434797.1; ENSG00000120925.16. [Q96K19-1]
DR Ensembl; ENST00000534961.5; ENSP00000445725.1; ENSG00000120925.16. [Q96K19-1]
DR GeneID; 81790; -.
DR KEGG; hsa:81790; -.
DR MANE-Select; ENST00000527424.6; ENSP00000434797.1; NM_030954.4; NP_112216.3.
DR UCSC; uc003xpm.4; human. [Q96K19-1]
DR CTD; 81790; -.
DR DisGeNET; 81790; -.
DR GeneCards; RNF170; -.
DR HGNC; HGNC:25358; RNF170.
DR HPA; ENSG00000120925; Low tissue specificity.
DR MalaCards; RNF170; -.
DR MIM; 608984; phenotype.
DR MIM; 614649; gene.
DR neXtProt; NX_Q96K19; -.
DR OpenTargets; ENSG00000120925; -.
DR PharmGKB; PA134922560; -.
DR VEuPathDB; HostDB:ENSG00000120925; -.
DR eggNOG; KOG2164; Eukaryota.
DR GeneTree; ENSGT00390000017123; -.
DR HOGENOM; CLU_1365859_0_0_1; -.
DR InParanoid; Q96K19; -.
DR OMA; CRQEEQN; -.
DR OrthoDB; 1563172at2759; -.
DR PhylomeDB; Q96K19; -.
DR TreeFam; TF328342; -.
DR PathwayCommons; Q96K19; -.
DR SignaLink; Q96K19; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 81790; 6 hits in 1116 CRISPR screens.
DR ChiTaRS; RNF170; human.
DR GenomeRNAi; 81790; -.
DR Pharos; Q96K19; Tbio.
DR PRO; PR:Q96K19; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96K19; protein.
DR Bgee; ENSG00000120925; Expressed in lateral nuclear group of thalamus and 198 other tissues.
DR ExpressionAtlas; Q96K19; baseline and differential.
DR Genevisible; Q96K19; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR010652; DUF1232.
DR InterPro; IPR038896; RNF170.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22894; PTHR22894; 1.
DR PANTHER; PTHR22894:SF1; PTHR22894:SF1; 1.
DR Pfam; PF06803; DUF1232; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endoplasmic reticulum; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..258
FT /note="E3 ubiquitin-protein ligase RNF170"
FT /id="PRO_0000280700"
FT TOPO_DOM 1..24
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 87..130
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023851"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044556"
FT VAR_SEQ 97..132
FT /note="PVETNCGHLFCGACIIAYWRYGSWLGAISCPICRQT -> MHLLPLDSSSTL
FT TCTVPSACTKPPSRWRPTVDIFFV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023852"
FT VAR_SEQ 109..116
FT /note="ACIIAYWR -> NLTPNSIW (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023853"
FT VAR_SEQ 117..258
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023854"
FT VAR_SEQ 133..200
FT /note="VTLLLTVFGEDDQSQDVLRLHQDINDYNRRFSGQPRSIMERIMDLPTLLRHA
FT FREMFSVGGLFWMFRI -> GSSEKSSRASEQTHQEAVACLDTQNSPACTVGCRSGPQH
FT IPHDRMLPSASPRLCFTLLDCVSILWFSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023855"
FT VAR_SEQ 170..258
FT /note="IMERIMDLPTLLRHAFREMFSVGGLFWMFRIRIILCLMGAFFYLISPLDFVP
FT EALFGILGFLDDFFVIFLLLIYISIMYREVITQRLTR -> VSNAKACSKLEEDTFLLF
FT CKVRFTNKYSLTMRNLGQAQWLAPIVLALWEAKAGGSLEPRSLRPALET (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023856"
FT VAR_SEQ 201..258
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023857"
FT VARIANT 199
FT /note="R -> C (in SNAX1; dbSNP:rs397514478)"
FT /evidence="ECO:0000269|PubMed:21115467"
FT /id="VAR_068219"
FT CONFLICT 9
FT /note="Q -> H (in Ref. 1; BAB55340)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="P -> T (in Ref. 4; AAH44566)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="P -> Q (in Ref. 4; AAH44566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 29815 MW; D87C0B0C121AFD76 CRC64;
MAKYQGEVQS LKLDDDSVIE GVSDQVLVAV VVSFALIATL VYALFRNVHQ NIHPENQELV
RVLREQLQTE QDAPAATRQQ FYTDMYCPIC LHQASFPVET NCGHLFCGAC IIAYWRYGSW
LGAISCPICR QTVTLLLTVF GEDDQSQDVL RLHQDINDYN RRFSGQPRSI MERIMDLPTL
LRHAFREMFS VGGLFWMFRI RIILCLMGAF FYLISPLDFV PEALFGILGF LDDFFVIFLL
LIYISIMYRE VITQRLTR
