AMGO1_HUMAN
ID AMGO1_HUMAN Reviewed; 493 AA.
AC Q86WK6; B4DIM3; Q8IW71; Q9ULQ7;
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|HGNC:HGNC:20824};
GN Synonyms=ALI2 {ECO:0000250|UniProtKB:Q80ZD8},
GN AMIGO {ECO:0000303|PubMed:12629050},
GN KIAA1163 {ECO:0000312|EMBL:BAA86477.1};
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] {ECO:0000312|EMBL:AAO48948.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Monocytic leukemia {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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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] {ECO:0000312|EMBL:AAH40879.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:AAH40879.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAA86477.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-493.
RC TISSUE=Brain {ECO:0000312|EMBL:BAA86477.1};
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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. Assembled with
CC KCNB1 modulates the gating characteristics of the delayed rectifier
CC voltage-dependent potassium channel KCNB1.
CC {ECO:0000250|UniProtKB:Q80ZD7, ECO:0000250|UniProtKB:Q80ZD8}.
CC -!- SUBUNIT: Homodimer, and heterodimer with AMIGO2 and AMIGO3. Interacts
CC with KCNB1. {ECO:0000250, ECO:0000250|UniProtKB:Q80ZD8}.
CC -!- INTERACTION:
CC Q86WK6; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-19125216, EBI-10827839;
CC Q86WK6; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-19125216, EBI-12109402;
CC Q86WK6; P07306: ASGR1; NbExp=3; IntAct=EBI-19125216, EBI-1172335;
CC Q86WK6; Q12983: BNIP3; NbExp=3; IntAct=EBI-19125216, EBI-749464;
CC Q86WK6; O14523: C2CD2L; NbExp=3; IntAct=EBI-19125216, EBI-12822627;
CC Q86WK6; O75508: CLDN11; NbExp=3; IntAct=EBI-19125216, EBI-12820543;
CC Q86WK6; O95484: CLDN9; NbExp=3; IntAct=EBI-19125216, EBI-18341636;
CC Q86WK6; Q07325: CXCL9; NbExp=3; IntAct=EBI-19125216, EBI-3911467;
CC Q86WK6; P56851: EDDM3B; NbExp=3; IntAct=EBI-19125216, EBI-10215665;
CC Q86WK6; Q92520: FAM3C; NbExp=3; IntAct=EBI-19125216, EBI-2876774;
CC Q86WK6; P29033: GJB2; NbExp=3; IntAct=EBI-19125216, EBI-3905204;
CC Q86WK6; Q9HCP6: HHATL; NbExp=3; IntAct=EBI-19125216, EBI-5916693;
CC Q86WK6; P24593: IGFBP5; NbExp=3; IntAct=EBI-19125216, EBI-720480;
CC Q86WK6; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-19125216, EBI-11742507;
CC Q86WK6; Q13021: MALL; NbExp=3; IntAct=EBI-19125216, EBI-750078;
CC Q86WK6; P30301: MIP; NbExp=3; IntAct=EBI-19125216, EBI-8449636;
CC Q86WK6; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-19125216, EBI-10317425;
CC Q86WK6; Q16617: NKG7; NbExp=3; IntAct=EBI-19125216, EBI-3919611;
CC Q86WK6; P0DJD7: PGA4; NbExp=3; IntAct=EBI-19125216, EBI-12957629;
CC Q86WK6; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-19125216, EBI-12092917;
CC Q86WK6; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-19125216, EBI-11721828;
CC Q86WK6; Q8N271: PROM2; NbExp=3; IntAct=EBI-19125216, EBI-18210782;
CC Q86WK6; P53801: PTTG1IP; NbExp=3; IntAct=EBI-19125216, EBI-3906138;
CC Q86WK6; Q9NS64: RPRM; NbExp=3; IntAct=EBI-19125216, EBI-1052363;
CC Q86WK6; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-19125216, EBI-9679163;
CC Q86WK6; Q9H2H9: SLC38A1; NbExp=3; IntAct=EBI-19125216, EBI-9978441;
CC Q86WK6; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-19125216, EBI-10314552;
CC Q86WK6; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-19125216, EBI-12266234;
CC Q86WK6; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-19125216, EBI-10290130;
CC Q86WK6; Q9UNK0: STX8; NbExp=3; IntAct=EBI-19125216, EBI-727240;
CC Q86WK6; O14894: TM4SF5; NbExp=3; IntAct=EBI-19125216, EBI-19125949;
CC Q86WK6; P56557: TMEM50B; NbExp=3; IntAct=EBI-19125216, EBI-12366453;
CC Q86WK6; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-19125216, EBI-2852148;
CC Q86WK6; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-19125216, EBI-8649725;
CC Q86WK6; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-19125216, EBI-12003398;
CC Q86WK6; P30536: TSPO; NbExp=3; IntAct=EBI-19125216, EBI-6623146;
CC Q86WK6; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-19125216, EBI-10243654;
CC Q86WK6; O00526: UPK2; NbExp=3; IntAct=EBI-19125216, EBI-10179682;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80ZD8};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q80ZD8}.
CC Perikaryon {ECO:0000250|UniProtKB:Q80ZD8}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q80ZD8}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q80ZD7}. Note=Colocalizes with KCNB1 at high-
CC density somatodendritic clusters on the surface of hippocampal and
CC cortical neurons. Associated with axons of neuronal cells.
CC {ECO:0000250|UniProtKB:Q80ZD7, ECO:0000250|UniProtKB:Q80ZD8}.
CC -!- DOMAIN: The LRR repeat region mediates homodimerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC {ECO:0000305}.
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DR EMBL; AY237007; AAO48948.1; -; mRNA.
DR EMBL; AK295678; BAG58535.1; -; mRNA.
DR EMBL; AL355145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040879; AAH40879.1; -; mRNA.
DR EMBL; AB032989; BAA86477.1; -; mRNA.
DR CCDS; CCDS30795.1; -.
DR RefSeq; NP_065754.2; NM_020703.2.
DR RefSeq; XP_011540114.1; XM_011541812.2.
DR AlphaFoldDB; Q86WK6; -.
DR SMR; Q86WK6; -.
DR BioGRID; 121533; 148.
DR IntAct; Q86WK6; 61.
DR STRING; 9606.ENSP00000358880; -.
DR TCDB; 8.A.43.1.10; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR GlyGen; Q86WK6; 5 sites.
DR iPTMnet; Q86WK6; -.
DR PhosphoSitePlus; Q86WK6; -.
DR BioMuta; AMIGO1; -.
DR DMDM; 68052342; -.
DR EPD; Q86WK6; -.
DR MassIVE; Q86WK6; -.
DR MaxQB; Q86WK6; -.
DR PaxDb; Q86WK6; -.
DR PeptideAtlas; Q86WK6; -.
DR PRIDE; Q86WK6; -.
DR ProteomicsDB; 70178; -.
DR ABCD; Q86WK6; 4 sequenced antibodies.
DR Antibodypedia; 53745; 339 antibodies from 34 providers.
DR DNASU; 57463; -.
DR Ensembl; ENST00000369862.1; ENSP00000358878.1; ENSG00000181754.7.
DR Ensembl; ENST00000369864.5; ENSP00000358880.4; ENSG00000181754.7.
DR GeneID; 57463; -.
DR KEGG; hsa:57463; -.
DR MANE-Select; ENST00000369864.5; ENSP00000358880.4; NM_020703.4; NP_065754.2.
DR UCSC; uc001dxx.5; human.
DR CTD; 57463; -.
DR DisGeNET; 57463; -.
DR GeneCards; AMIGO1; -.
DR HGNC; HGNC:20824; AMIGO1.
DR HPA; ENSG00000181754; Low tissue specificity.
DR MIM; 615689; gene.
DR neXtProt; NX_Q86WK6; -.
DR OpenTargets; ENSG00000181754; -.
DR PharmGKB; PA142672625; -.
DR VEuPathDB; HostDB:ENSG00000181754; -.
DR eggNOG; ENOG502QVUQ; Eukaryota.
DR GeneTree; ENSGT00950000183146; -.
DR HOGENOM; CLU_030478_0_0_1; -.
DR InParanoid; Q86WK6; -.
DR OMA; VFSDTPM; -.
DR OrthoDB; 671228at2759; -.
DR PhylomeDB; Q86WK6; -.
DR TreeFam; TF326838; -.
DR PathwayCommons; Q86WK6; -.
DR SignaLink; Q86WK6; -.
DR BioGRID-ORCS; 57463; 25 hits in 1066 CRISPR screens.
DR ChiTaRS; AMIGO1; human.
DR GenomeRNAi; 57463; -.
DR Pharos; Q86WK6; Tbio.
DR PRO; PR:Q86WK6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86WK6; protein.
DR Bgee; ENSG00000181754; Expressed in middle temporal gyrus and 160 other tissues.
DR Genevisible; Q86WK6; HS.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:1990030; C:pericellular basket; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl.
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:0050772; P:positive regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IEA:Ensembl.
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; 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; 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 Cell adhesion; Cell membrane; Cell projection; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..493
FT /note="Amphoterin-induced protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014506"
FT TOPO_DOM 28..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..61
FT /note="LRRNT"
FT REPEAT 62..83
FT /note="LRR 1"
FT REPEAT 87..108
FT /note="LRR 2"
FT REPEAT 111..132
FT /note="LRR 3"
FT REPEAT 135..156
FT /note="LRR 4"
FT REPEAT 159..179
FT /note="LRR 5"
FT REPEAT 186..206
FT /note="LRR 6"
FT DOMAIN 221..272
FT /note="LRRCT"
FT DOMAIN 269..353
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT REGION 405..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80ZD8"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 38..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 225..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 227..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 290..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 454
FT /note="N -> S (in Ref. 4; AAH40879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 55239 MW; 8685B358570D9455 CRC64;
MHPHRDPRGL WLLLPSLSLL LFEVARAGRA VVSCPAACLC ASNILSCSKQ QLPNVPHSLP
SYTALLDLSH NNLSRLRAEW TPTRLTQLHS LLLSHNHLNF ISSEAFSPVP NLRYLDLSSN
QLRTLDEFLF SDLQVLEVLL LYNNHIMAVD RCAFDDMAQL QKLYLSQNQI SRFPLELVKE
GAKLPKLTLL DLSSNKLKNL PLPDLQKLPA WIKNGLYLHN NPLNCDCELY QLFSHWQYRQ
LSSVMDFQED LYCMNSKKLH NVFNLSFLNC GEYKERAWEA HLGDTLIIKC DTKQQGMTKV
WVTPSNERVL DEVTNGTVSV SKDGSLLFQQ VQVEDGGVYT CYAMGETFNE TLSVELKVHN
FTLHGHHDTL NTAYTTLVGC ILSVVLVLIY LYLTPCRCWC RGVEKPSSHQ GDSLSSSMLS
TTPNHDPMAG GDKDDGFDRR VAFLEPAGPG QGQNGKLKPG NTLPVPEATG KGQRRMSDPE
SVSSVFSDTP IVV
