AMGO1_MOUSE
ID AMGO1_MOUSE Reviewed; 492 AA.
AC Q80ZD8; A2AE40; Q69ZQ0; Q8R5D4; Q921U9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Amphoterin-induced protein 1;
DE AltName: Full=AMIGO-1;
DE AltName: Full=Alivin-2;
DE Flags: Precursor;
GN Name=Amigo1 {ECO:0000312|MGI:MGI:2653612};
GN Synonyms=Ali2 {ECO:0000312|EMBL:BAD12541.1},
GN Amigo {ECO:0000303|PubMed:12629050},
GN Kiaa1163 {ECO:0000312|EMBL:BAD32396.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAO48949.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO48949.1};
RC TISSUE=Brain {ECO:0000269|PubMed:12629050};
RX PubMed=12629050; DOI=10.1083/jcb.200209074;
RA Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A., Rauvala H.;
RT "AMIGO, a transmembrane protein implicated in axon tract development,
RT defines a novel protein family with leucine-rich repeats.";
RL J. Cell Biol. 160:963-973(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD12541.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAD12541.1};
RA Ono T.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAD32396.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD32396.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH10598.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH10598.2};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH10598.2};
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476 AND SER-480, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
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).
RN [8]
RP FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22056818; DOI=10.1038/embor.2011.204;
RA Peltola M.A., Kuja-Panula J., Lauri S.E., Taira T., Rauvala H.;
RT "AMIGO is an auxiliary subunit of the Kv2.1 potassium channel.";
RL EMBO Rep. 12:1293-1299(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-370, DISULFIDE BONDS,
RP LEUCINE-RICH REPEATS, SUBUNIT, GLYCOSYLATION AT ASN-72; ASN-269; ASN-315;
RP ASN-348 AND ASN-359, MUTAGENESIS OF ASN-348, AND SUBCELLULAR LOCATION.
RX PubMed=21983541; DOI=10.1016/j.jmb.2011.09.032;
RA Kajander T., Kuja-Panula J., Rauvala H., Goldman A.;
RT "Crystal structure and role of glycans and dimerization in folding of
RT neuronal leucine-rich repeat protein AMIGO-1.";
RL J. Mol. Biol. 413:1001-1015(2011).
CC -!- FUNCTION: Promotes growth and fasciculation of neurites from cultured
CC hippocampal neurons. May be involved in fasciculation as well as
CC myelination of developing neural axons. May have a role in regeneration
CC as well as neural plasticity in the adult nervous system. May mediate
CC homophilic as well as heterophilic cell-cell interaction and contribute
CC to signal transduction through its intracellular domain (By
CC similarity). Assembled with KCNB1 modulates the gating characteristics
CC of the delayed rectifier voltage-dependent potassium channel KCNB1
CC (PubMed:22056818). {ECO:0000250|UniProtKB:Q80ZD7,
CC ECO:0000269|PubMed:22056818}.
CC -!- SUBUNIT: Homodimer, and heterodimer with AMIGO2 and AMIGO3
CC (PubMed:21983541). Interacts with KCNB1 (PubMed:22056818).
CC {ECO:0000269|PubMed:21983541, ECO:0000269|PubMed:22056818}.
CC -!- INTERACTION:
CC Q80ZD8; Q03717: Kcnb1; NbExp=4; IntAct=EBI-7511393, EBI-7511364;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21983541,
CC ECO:0000269|PubMed:22056818}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:21983541}. Perikaryon
CC {ECO:0000269|PubMed:22056818}. Cell projection, dendrite
CC {ECO:0000269|PubMed:22056818}. Note=Colocalizes with KCNB1 at high-
CC density somatodendritic clusters on the surface of hippocampal and
CC cortical neurons (PubMed:22056818). Associated with axons of neuronal
CC cells (By similarity). {ECO:0000250|UniProtKB:Q80ZD7,
CC ECO:0000269|PubMed:22056818}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12629050};
CC IsoId=Q80ZD8-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q80ZD8-2; Sequence=VSP_014166, VSP_014167;
CC -!- TISSUE SPECIFICITY: Expressed in hippocampal and cortical neurons (at
CC protein level) (PubMed:22056818). High levels in cerebellum, cerebrum,
CC and retina. Low levels in liver, kidney, small intestine, spleen, lung
CC and heart. {ECO:0000269|PubMed:12629050, ECO:0000269|PubMed:22056818}.
CC -!- DOMAIN: The LRR repeat region mediates homodimerization.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22907.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD32396.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY237008; AAO48949.1; -; mRNA.
DR EMBL; AB167509; BAD12541.1; -; mRNA.
DR EMBL; AK035960; BAC29259.1; -; mRNA.
DR EMBL; AK173118; BAD32396.1; ALT_INIT; mRNA.
DR EMBL; AL671854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010598; AAH10598.2; -; mRNA.
DR EMBL; BC022907; AAH22907.1; ALT_FRAME; mRNA.
DR CCDS; CCDS17753.1; -. [Q80ZD8-1]
DR CCDS; CCDS71305.1; -. [Q80ZD8-2]
DR RefSeq; NP_001004293.1; NM_001004293.2. [Q80ZD8-1]
DR RefSeq; NP_001274022.1; NM_001287093.1. [Q80ZD8-2]
DR RefSeq; NP_666249.2; NM_146137.3. [Q80ZD8-1]
DR PDB; 2XOT; X-ray; 2.00 A; A/B=28-370.
DR PDBsum; 2XOT; -.
DR AlphaFoldDB; Q80ZD8; -.
DR SMR; Q80ZD8; -.
DR BioGRID; 230893; 5.
DR IntAct; Q80ZD8; 1.
DR MINT; Q80ZD8; -.
DR STRING; 10090.ENSMUSP00000102267; -.
DR GlyConnect; 2127; 1 N-Linked glycan (1 site).
DR GlyGen; Q80ZD8; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q80ZD8; -.
DR PhosphoSitePlus; Q80ZD8; -.
DR PaxDb; Q80ZD8; -.
DR PeptideAtlas; Q80ZD8; -.
DR PRIDE; Q80ZD8; -.
DR ProteomicsDB; 296201; -. [Q80ZD8-1]
DR ProteomicsDB; 296202; -. [Q80ZD8-2]
DR ABCD; Q80ZD8; 6 sequenced antibodies.
DR Antibodypedia; 53745; 339 antibodies from 34 providers.
DR DNASU; 229715; -.
DR Ensembl; ENSMUST00000050909; ENSMUSP00000061244; ENSMUSG00000050947. [Q80ZD8-1]
DR Ensembl; ENSMUST00000106656; ENSMUSP00000102267; ENSMUSG00000050947. [Q80ZD8-1]
DR Ensembl; ENSMUST00000106659; ENSMUSP00000102270; ENSMUSG00000050947. [Q80ZD8-2]
DR GeneID; 229715; -.
DR KEGG; mmu:229715; -.
DR UCSC; uc008qyg.2; mouse. [Q80ZD8-1]
DR UCSC; uc033hze.1; mouse. [Q80ZD8-2]
DR CTD; 57463; -.
DR MGI; MGI:2653612; Amigo1.
DR VEuPathDB; HostDB:ENSMUSG00000050947; -.
DR eggNOG; ENOG502QVUQ; Eukaryota.
DR GeneTree; ENSGT00950000183146; -.
DR HOGENOM; CLU_030478_0_0_1; -.
DR InParanoid; Q80ZD8; -.
DR OMA; WLRDRLY; -.
DR OrthoDB; 671228at2759; -.
DR TreeFam; TF326838; -.
DR BioGRID-ORCS; 229715; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q80ZD8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80ZD8; protein.
DR Bgee; ENSMUSG00000050947; Expressed in dentate gyrus of hippocampal formation granule cell and 145 other tissues.
DR ExpressionAtlas; Q80ZD8; baseline and differential.
DR Genevisible; Q80ZD8; MM.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:1990030; C:pericellular basket; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISO:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:1905232; P:cellular response to L-glutamate; ISO:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0106030; P:neuron projection fasciculation; ISO:MGI.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR031283; AMIGO.
DR InterPro; IPR031284; AMIGO1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR24368; PTHR24368; 1.
DR PANTHER; PTHR24368:SF1; PTHR24368:SF1; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Neurogenesis; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..492
FT /note="Amphoterin-induced protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014507"
FT TOPO_DOM 28..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..61
FT /note="LRRNT"
FT REPEAT 62..83
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:21983541"
FT REPEAT 87..108
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:21983541"
FT REPEAT 111..132
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:21983541"
FT REPEAT 135..156
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:21983541"
FT REPEAT 159..180
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:21983541"
FT REPEAT 186..206
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:21983541"
FT DOMAIN 208..272
FT /note="LRRCT"
FT DOMAIN 269..352
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT REGION 404..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21983541"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21983541"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21983541"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21983541"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21983541"
FT DISULFID 34..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21983541"
FT DISULFID 38..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21983541"
FT DISULFID 225..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21983541"
FT DISULFID 227..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21983541"
FT DISULFID 290..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21983541"
FT VAR_SEQ 290..309
FT /note="CDTKQQGMTKVWVSPSNEQV -> TLPPTVYTRLANLRAHGLYN (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014166"
FT VAR_SEQ 310..492
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014167"
FT MUTAGEN 348
FT /note="N->A: Prevents from leaving the ER."
FT /evidence="ECO:0000269|PubMed:21983541"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2XOT"
FT TURN 103..108
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2XOT"
FT TURN 127..132
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2XOT"
FT TURN 151..156
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2XOT"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2XOT"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:2XOT"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2XOT"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:2XOT"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:2XOT"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:2XOT"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:2XOT"
FT STRAND 348..360
FT /evidence="ECO:0007829|PDB:2XOT"
SQ SEQUENCE 492 AA; 55343 MW; EF1CCD6BA61FE222 CRC64;
MQPQRDLRGL WLLLLSVFLL LFEVARAGRS VVSCPANCLC ASNILSCSKQ QLPNVPQSLP
SYTALLDLSH NNLSRLRAEW TPTRLTNLHS LLLSHNHLNF ISSEAFVPVP NLRYLDLSSN
HLHTLDEFLF SDLQALEVLL LYNNHIVVVD RNAFEDMAQL QKLYLSQNQI SRFPVELIKD
GNKLPKLMLL DLSSNKLKKL PLTDLQKLPA WVKNGLYLHN NPLECDCKLY QLFSHWQYRQ
LSSVMDFQED LYCMHSKKLH NIFSLDFFNC SEYKESAWEA HLGDTLTIRC DTKQQGMTKV
WVSPSNEQVL SQGSNGSVSV RNGDLFFKKV QVEDGGVYTC YAMGETFNET LSVELKVYNF
TLHGHHDTLN TAYTTLVGCI LSVVLVLIYL YLTPCRCWCR GVEKPSSHQG DSLSSSMLST
TPNHDPMAGG DKDDGFDRRV AFLEPAGPGQ GQNGKLKPGN TLPVPEATGK GQRRMSDPES
VSSVFSDTPI VV
