RN216_MOUSE
ID RN216_MOUSE Reviewed; 853 AA.
AC P58283; Q3U493; Q3UE56; Q3UGM3; Q68FN0; Q6P1H8; Q6PWY5; Q8BN27; Q8C1U3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=E3 ubiquitin-protein ligase RNF216;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 216;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF216 {ECO:0000305};
DE AltName: Full=Triad domain-containing protein 3;
DE AltName: Full=UbcM4-interacting protein 83;
DE AltName: Full=Ubiquitin-conjugating enzyme 7-interacting protein 1;
GN Name=Rnf216; Synonyms=Triad3, Ubce7ip1, Uip83, Zin;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RA Chuang T.H., Ulevitch R.J.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow macrophage, Dendritic cell, Melanocyte, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 448-593, AND INTERACTION WITH UBE2L3.
RC STRAIN=CD-1; TISSUE=Embryo;
RX PubMed=10431818; DOI=10.1016/s0014-5793(99)00823-6;
RA Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.;
RT "A family of structurally related RING finger proteins interacts
RT specifically with the ubiquitin-conjugating enzyme UbcM4.";
RL FEBS Lett. 454:257-261(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as an E3 ubiquitin ligase, which accepts ubiquitin from
CC specific E2 ubiquitin-conjugating enzymes, and then transfers it to
CC substrates promoting their degradation by the proteasome. Promotes
CC degradation of TRAF3, TLR4 and TLR9. Contributes to the regulation of
CC antiviral responses. Down-regulates activation of NF-kappa-B, IRF3
CC activation and IFNB production. Promotes TNF and RIP mediated
CC apoptosis. {ECO:0000250|UniProtKB:Q9NWF9}.
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: Interacts with UBE2L3 and to some extent with UBE2L6.
CC Interacts with RIPK1, TRAF3, TLR3, TLR4, TLR5 and TLR9. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=TRIAD3A, a;
CC IsoId=P58283-1; Sequence=Displayed;
CC Name=2; Synonyms=TRIAD3B, b;
CC IsoId=P58283-2; Sequence=VSP_007408;
CC Name=3;
CC IsoId=P58283-3; Sequence=VSP_019293, VSP_019294;
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
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DR EMBL; AY572785; AAS78930.1; -; mRNA.
DR EMBL; AY572786; AAS78931.1; -; mRNA.
DR EMBL; AK089775; BAC40959.1; -; mRNA.
DR EMBL; AK147861; BAE28184.1; -; mRNA.
DR EMBL; AK149741; BAE29055.1; -; mRNA.
DR EMBL; AK154368; BAE32540.1; -; mRNA.
DR EMBL; BC065066; AAH65066.1; -; mRNA.
DR EMBL; BC079540; AAH79540.1; -; mRNA.
DR EMBL; AF361000; AAK51470.1; -; mRNA.
DR CCDS; CCDS57400.1; -. [P58283-2]
DR CCDS; CCDS80455.1; -. [P58283-1]
DR RefSeq; NP_542128.2; NM_080561.4. [P58283-1]
DR RefSeq; NP_996993.1; NM_207110.1. [P58283-2]
DR RefSeq; XP_006504707.1; XM_006504644.3. [P58283-2]
DR RefSeq; XP_006504708.1; XM_006504645.3. [P58283-1]
DR RefSeq; XP_017176080.1; XM_017320591.1. [P58283-2]
DR AlphaFoldDB; P58283; -.
DR SMR; P58283; -.
DR BioGRID; 223823; 7.
DR STRING; 10090.ENSMUSP00000052563; -.
DR iPTMnet; P58283; -.
DR PhosphoSitePlus; P58283; -.
DR EPD; P58283; -.
DR MaxQB; P58283; -.
DR PeptideAtlas; P58283; -.
DR PRIDE; P58283; -.
DR ProteomicsDB; 300541; -. [P58283-1]
DR ProteomicsDB; 300542; -. [P58283-2]
DR ProteomicsDB; 300543; -. [P58283-3]
DR Antibodypedia; 11455; 215 antibodies from 28 providers.
DR DNASU; 108086; -.
DR Ensembl; ENSMUST00000053498; ENSMUSP00000052563; ENSMUSG00000045078. [P58283-1]
DR Ensembl; ENSMUST00000200607; ENSMUSP00000143705; ENSMUSG00000045078. [P58283-2]
DR GeneID; 108086; -.
DR KEGG; mmu:108086; -.
DR UCSC; uc009ajm.2; mouse. [P58283-1]
DR UCSC; uc009ajn.2; mouse. [P58283-2]
DR UCSC; uc009ajo.2; mouse. [P58283-3]
DR CTD; 54476; -.
DR MGI; MGI:1344349; Rnf216.
DR VEuPathDB; HostDB:ENSMUSG00000045078; -.
DR eggNOG; KOG1812; Eukaryota.
DR GeneTree; ENSGT00510000048032; -.
DR HOGENOM; CLU_011576_1_0_1; -.
DR InParanoid; P58283; -.
DR OMA; MDGNCTC; -.
DR OrthoDB; 1486032at2759; -.
DR PhylomeDB; P58283; -.
DR TreeFam; TF330852; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 108086; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Rnf216; mouse.
DR PRO; PR:P58283; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P58283; protein.
DR Bgee; ENSMUSG00000045078; Expressed in spermatid and 227 other tissues.
DR ExpressionAtlas; P58283; baseline and differential.
DR Genevisible; P58283; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0098843; C:postsynaptic endocytic zone; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0099546; P:protein catabolic process, modulating synaptic transmission; ISO:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0050691; P:regulation of defense response to virus by host; ISS:UniProtKB.
DR GO; GO:0032648; P:regulation of interferon-beta production; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00647; IBR; 2.
DR PROSITE; PS51873; TRIAD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Coiled coil; Cytoplasm; Isopeptide bond;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..853
FT /note="E3 ubiquitin-protein ligase RNF216"
FT /id="PRO_0000056294"
FT ZN_FING 503..552
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 571..636
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 663..691
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 33..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..716
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT COILED 463..479
FT /evidence="ECO:0000255"
FT COILED 725..751
FT /evidence="ECO:0000255"
FT COMPBIAS 53..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 503
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 593
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 611
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 616
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 621
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 631
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 636
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 683
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 688
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 704
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 712
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 436
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 447
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 607
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 646
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 753
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT CROSSLNK 761
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWF9"
FT VAR_SEQ 66
FT /note="E -> ETHKPQTSRPNLIKPAAQWQDLNRLGEERPRKSRADFEADIHNYFSF
FT CNNSLFGSGAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_007408"
FT VAR_SEQ 619..732
FT /note="ETCRKCQGLWKEHNGLTCEELAEKDDIKYRTSIEEKMTAARIRKCHKCGTGL
FT IKSEGCNRMSCRCGAQMCYLCRVSINGYDHFCQHPRSPGAPCQECSRCSLWTDPTEDDE
FT KLI -> VRRTVVCVSSTLLEFGLHYAGGLCRLMHENSLPLPFMKQEKVGDGSWHSYRD
FT EITCGNPIAKFRISRLCHFIKTGAVKMCLLLLCRIFCLLFSLSCTQIQHIHTCKLGKIC
FT MDI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019293"
FT VAR_SEQ 733..853
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019294"
FT CONFLICT 377
FT /note="D -> A (in Ref. 2; BAE32540)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="K -> R (in Ref. 2; BAE28184)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="A -> V (in Ref. 2; BAE28184)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="K -> E (in Ref. 2; BAE28184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 853 AA; 97682 MW; 3EFE484C5AA5E0B8 CRC64;
MAEGNNKEEV IHLNNFPCHR GKEWMAVREG PITISDSSDE EGIPMLVTPA TEQQEDDLDD
DVILTEDDSE DEYGGFLDLE SGKKEGEAKP GPSSKQTADD IVNPRLEQKV IILGENGLLF
PESEPLEVQN QSSEDSETEL LSNPGEPAAS VDDQLIGEEY WLDHPYFQAP NPQPQERTNQ
VVPQERHSES EMGPMFFRHD FPEPAFPRPE PQQEGIPGPA SPQPAHPLGE LEDQQLAIDE
DPGPAFPLSG PQEANLANMW EQEAAEVDQD LIPLLVKETE ARFPDVASGY VEEIIHLKNY
YDLNVLCNFL LENPDYPKRE DRLIIHPSSS LLASQDDAKL PKIDFFDYSK LTPLDQRCFI
QAADLLMADF KMLSSQDIKW ALHELKGHYA ITRKAFSDAI KKWQELSPET SGKRKKRKEM
NQYSFIDFKF EQGNIKIEKR MFFLENKRRH CRYYDHQALL PAVKQEQEFY EQKIKEMAEH
EDFLLALQMN EEQYQKDGQL IECRCCYGEF PFEELTQCAD AHLFCKECLI RYAQEAVFGS
GKSELSCMEG SCTCSFPTSE LEKVLPQTIL YKYYERKAEE EVAAAYADEL VRCPSCSFPA
LLDSDVKRFS CPNPRCRKET CRKCQGLWKE HNGLTCEELA EKDDIKYRTS IEEKMTAARI
RKCHKCGTGL IKSEGCNRMS CRCGAQMCYL CRVSINGYDH FCQHPRSPGA PCQECSRCSL
WTDPTEDDEK LIEEIQKEAE EEQKRKNGEN TFKRIGPPLE KPAEKVQRVE ALPRPVPQNL
HPQMPPYAFV HPPFPLPPVR PVFNNFPINM GPVPAPYVPP LPNVRVNYDF GHMHVPLEHN
LPMHFGPQPR HRF
