EYS_PONAB
ID EYS_PONAB Reviewed; 3164 AA.
AC Q5R6R1; A0A2J8XWZ5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 3.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein eyes shut homolog;
DE AltName: Full=Epidermal growth factor-like protein 10;
DE Short=EGF-like protein 10;
DE AltName: Full=Epidermal growth factor-like protein 11;
DE Short=EGF-like protein 11;
DE AltName: Full=Protein spacemaker homolog;
DE Flags: Precursor;
GN Name=EYS; Synonyms=EGFL10, EGFL11, SPAM;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie;
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2230-3164 (ISOFORM 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required to maintain the integrity of photoreceptor cells (By
CC similarity). Specifically required for normal morphology of the
CC photoreceptor ciliary pocket, and might thus facilitate protein
CC trafficking between the photoreceptor inner and outer segments via the
CC transition zone (By similarity). {ECO:0000250|UniProtKB:B8JI71,
CC ECO:0000250|UniProtKB:Q5T1H1}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000250|UniProtKB:Q5T1H1}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q5T1H1}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:A0A2K5V015}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q5T1H1}. Secreted, extracellular space,
CC extracellular matrix, interphotoreceptor matrix
CC {ECO:0000250|UniProtKB:Q5T1H1}. Note=Localizes to discrete puncta at,
CC or adjacent to, the photoreceptor connecting cilium. Highly expressed
CC in cone photoreceptor outer segments (By similarity). Weakly expressed
CC in rod photoreceptor outer segments (By similarity). May localize to
CC the cilium axoneme (By similarity). May also be secreted into the
CC interphotoreceptor extracellular matrix (By similarity).
CC {ECO:0000250|UniProtKB:A0A2K5V015, ECO:0000250|UniProtKB:Q5T1H1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R6R1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R6R1-2; Sequence=VSP_060083, VSP_060084;
CC -!- SIMILARITY: Belongs to the EYS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH92549.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; NDHI03003297; PNJ86529.1; -; Genomic_DNA.
DR EMBL; CR860424; CAH92549.1; ALT_INIT; mRNA.
DR RefSeq; NP_001126492.1; NM_001133020.1.
DR STRING; 9601.ENSPPYP00000018744; -.
DR Ensembl; ENSPPYT00000019479; ENSPPYP00000018737; ENSPPYG00000016753. [Q5R6R1-2]
DR Ensembl; ENSPPYT00000041207; ENSPPYP00000041122; ENSPPYG00000016753. [Q5R6R1-1]
DR GeneID; 100173479; -.
DR KEGG; pon:100173479; -.
DR CTD; 346007; -.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000163729; -.
DR InParanoid; Q5R6R1; -.
DR OrthoDB; 448591at2759; -.
DR Proteomes; UP000001595; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
DR CDD; cd00110; LamG; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00008; EGF; 10.
DR Pfam; PF12661; hEGF; 4.
DR Pfam; PF02210; Laminin_G_2; 5.
DR SMART; SM00181; EGF; 27.
DR SMART; SM00179; EGF_CA; 22.
DR SMART; SM00282; LamG; 5.
DR SUPFAM; SSF49899; SSF49899; 5.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00022; EGF_1; 21.
DR PROSITE; PS01186; EGF_2; 15.
DR PROSITE; PS50026; EGF_3; 27.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell projection; Cytoplasm; Cytoskeleton;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Sensory transduction; Signal; Vision.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..3164
FT /note="Protein eyes shut homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000341224"
FT DOMAIN 170..212
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 213..254
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 256..292
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 332..368
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 370..406
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 567..602
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 643..679
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 681..720
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 733..769
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 771..807
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 809..847
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 849..888
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 890..926
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 928..964
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 966..1002
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1004..1040
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1042..1077
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1079..1115
FT /note="EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1117..1159
FT /note="EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1161..1197
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1883..2063
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2099..2140
FT /note="EGF-like 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2145..2339
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2335..2368
FT /note="EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2371..2408
FT /note="EGF-like 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2419..2609
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2610..2646
FT /note="EGF-like 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2648..2689
FT /note="EGF-like 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2717..2895
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2896..2932
FT /note="EGF-like 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2933..2970
FT /note="EGF-like 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2975..3164
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 863
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1906
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2033
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2775
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2951
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2971
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3073
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3082
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 174..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 183..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 202..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 217..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 222..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 244..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 260..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 265..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 282..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 336..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 341..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 358..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 374..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 396..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 575..590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 592..601
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 652..667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 685..696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 690..705
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 707..719
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 737..748
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 742..757
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 775..786
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 780..795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 797..806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 813..824
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 818..835
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 837..846
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 853..866
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 860..876
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 878..887
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 894..905
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 899..914
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 916..925
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 932..943
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 937..952
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 954..963
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 970..981
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 975..990
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 992..1001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1008..1019
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1013..1028
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1030..1039
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1046..1056
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1051..1065
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1067..1076
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1083..1094
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1088..1103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1105..1114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1121..1137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1131..1147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1149..1158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1165..1176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1170..1185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1187..1196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2037..2063
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 2103..2114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2108..2128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2130..2139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2308..2339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 2339..2350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2344..2359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2375..2386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2380..2396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2398..2407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2576..2609
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 2614..2625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2619..2634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2636..2645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2652..2668
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2662..2677
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2679..2688
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2868..2895
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 2900..2911
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2905..2920
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2922..2931
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2937..2948
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2942..2958
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2960..2969
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 2691..2701
FT /note="ALILIVILEKP -> GHQFIGKDVFK (in isoform 2)"
FT /id="VSP_060083"
FT VAR_SEQ 2702..3164
FT /note="Missing (in isoform 2)"
FT /id="VSP_060084"
SQ SEQUENCE 3164 AA; 350638 MW; EC9B742D24EAEC1B CRC64;
MTDKSIIILS LMVFHSSFIN GKTCRRQSVE EWHPQPSSYV VNWTLTENIC LDFYRDCWFL
GVNTKIDTSG NQAVPQICPL QIQLGDILVI SSEPSLQFPE INLMNVSETS FIGCVQNTTT
EDQLLFGCRL KGMHTVNSKW LSVGTHYFIT VMASGPSPCP LGLRLNVTVK QQFCQESLSS
EFCSGHGKCL SEAWSKTYSC HCHPPFSGKY CQELDACSFK PCKNNGSCIN KRENWDGQGY
ECVCHPPFTG KNCSEIIGQC QPHVCFHGNC SNITSNSFIC ECDEQFSGPF CEMSTKPCVS
LLCWKRGICP NSSSAYTYEC PKGSSSQNGE TDVSECSLVP CQNGTDCIQI SNDVMCICSP
IFTDLLCKSI QTSCESFSLR NNATCKKWEK DYHCSCISGF TEKNCEKAID HCRLLSINCL
NEEWCFNIIG RFNYVCIPGC PKNPCWFLKN VYLIHQHLCY CGVTFHGICQ DKGPAQFEYV
WQLGFAGSEG EKCQGVIDAY FFLAANCTED AICVNDPEDY NSSCRFPREG TKEICANGCS
CLSEEDSQEY LYLCFLRWAG NMYLENTTDD QENECQHEAI CKDEINRPRC SCSLSYIGRL
CVVNVDYCLG NQSISVHGLC LALSHKCNCI SLQRYERNIC EIDTEDCKSV SCKNGTTSIH
LRGYFFCKCV PGFKGTQREI DIDECASHPC KNGATCIDQP GNYFCQCVPP FKVVDGFSCL
GNPGYVGIRC EQDIDDCILN ACEHNSTCKD LHLSYQCVCL SGWEGNFSEQ ESNECKMNPC
KNNSTCIDLY KSYRCECTSG WTGQNCSEEI NECDSDPCMN GGLCHESTIP GQFVCLCPPL
YTGRFCHQRY NPCDLLHNPC RNNSTCLALV DGNQHCICRE EFEGKNCEID VKECLFLSCQ
DYGDCEDMVN NFRCICRPGF SGSLCEIEIN ECSSEPCKNN GTCVDLTNRF FCNCEPGYHG
PFCELDVNKC KISPCLDEEN CVYRTDGYNC LCAPGYTGIN CEINLDECLS EPCLHDGVCI
DGINHYTCDC KSGFFGTHCE TNANDCLSNP CLHGRCTELI NEYPCSCDAD GTSTQCKIKI
NDCTSIPCMN EGFCQKSAHG FTCICPRGYT GAYCEKSIDN CAEPEFNSVI CLNGGICVDG
PGHTFDCRCL PGFSGQFCEI NINECSSSPC LHGADCEDHI NGYVCKCQPG WSGHHCEKEL
ECIPNSCVHE LCMENEPGST CLCTPGFMTC STGLLCGDEI RRITCLTPIF QRTDPISTQT
YTVPPSETLV SSFPSIKATR IPAIMDTYPV DQGPKQTGIV KHDILPTTGL AALRISTPLE
SYLLEELIVT RELSAKHGLL SSADVSSSRF LNFGIHDPAQ IVQDKTSVSH MPIRTSAATL
GFFFPDRRAR TPFIMSSVMS DFIFPTQSLL FENYQTVASS ATPTTSVIRS IPGADIELNR
QSLLSRGFLL TAASISATPV VSRGAQEDIE EYSADSLISR REHWRLLSPS MSPIFPAKII
ISKQVTILNS SALHRFGTKA FNPSEYQAIT EASSNQRLTN IKSQAADSLR ELSQTCATCS
MTEIKSSREF SDQVLHSKQS HFYETFWMNS AILASWCALM GAQTITSGHS FSSATEITPS
VAFTEVPSLF PSKKSAKRTI LSSSLEESIT LSSNLDVNLC LDKTCLSIVP SQTISSDLMN
SDLTSKMTTD ELSVSANILK LLKIRQYGIT MGPTEVLNQD SLLDMEKSKG SHTPFKLHPS
DSSLDFELNL QIYPDVTLKT YSEITHANDF KNTLPPLTGS VPDFSEVTTN VAFYTVSATP
ALSIQTSSSM SVIRPDWPYF TDYMTSLKKE VKTSSEWSKW ELQPSVQYQE FPTASWHLPF
TRSLTLSSLE SILAPQQLTI SDFSCVRYYG DSYLEFQNVV LNPQNNISLE FQTFSSYGLL
LYVKQDSNLV DGFFIQLFIE NGTLKYHFYC PGEAKFKSIN TTIRVDDGQK YTLLIRQELY
PCKAELTILG RNTQTCESIS HVLGKPLPKS GSVFIGGFPD LHGKIQMPVP VKNFTGCIEV
IEINNWRSFI PSKAVKNYHI NNCRSQGFML SPTASFVDVS DVTQGVDTMW TSVSPSVAAP
SVCQQDVCHN GGTCHPIFLS RGIVSFQCDC PLHFTGRFCE KDASLFFPSF NGNSYLELPF
LKFVLEKEHN RTVTIYLTIK TNSLNGTILY SNGNNFGKQF LHLFLVEGRP SVKYGCGNSQ
NILTVSANYS INTNAFTPIT IRYTTPVGSP GVVCMIEMTA DGKPPVQKKD TEISQASQAY
FESMFLGHIP ANVQIHKKSG PVYGFRGCIL DLQVNNKEFF IIDEARHGKN IENCHVPWCA
HHLCRNNGTC ISDNENLFCE CPRLYSGKLC QFASCENNPC GNGATCVPKS GTDIVCLCPY
GRSGPLCTDA INITQPRFSG TDAFGYTSFL AYSRISDISF HYEFHLKFQL ANNHSALQNN
LIFFTGQKGH GLNGDDFLAV GLLNGSVVYS YNLGSGIASI RSEPLNLSLG VHTVHLGKFF
QEGWLKVDDH KNKSIIAPGR LAGLNVFSQF YVGGYSEYTP DLLPNGADFK NGFQGCIFTL
QVRTEKDGHF RGLGNPEGHP NAGRSVGQCH ASPCSLMKCG NGGTCIESGT SVYCNCTTGW
KGAFCTETVS TCDPEHDPPH HCSRGATCIS LPHGYTCFCP LGTTGIYCEQ ALILIVILEK
PKPAEWKVKK EALSISDPSF RSNELSWMSF ASFHVRKKTH IQLQFQPLAA DGILFYAAQH
LKAQSGDFLC ISLVNSSVQL RYNLGDRTII LETLQKVTIN GSTWHIIKAG RVGAEGYLDL
DGINVTEKAS TKMSSLDTNT DFYIGGVSSL NLVNPMAIEN EPVGFQGCIR QVIINNQELQ
LTEFGAKGGS NVGDCDGTAC GYNTCRNGGE CTVNGTTFSC RCLPDWAGNT CNQSVYCLNN
LCLHQSLCIP NQSFSYSCLC TLGWVGRYCE NKTSFSTAKF MGNSYIKYID PNYRMRNLQF
TTISLNFSTT KTEGLIVWMG TAQNEENDFL AIGLHNQTLK IAVNLGERIS VPMSYNNGTF
CCNKWHHVVV IQNQTLIKAY VNNSLILSED IDPHKNFVAL NYDGICYLGG FEYGRKVSIV
TQEIFKTNFV GKIKDVFFQD PKKIELIKLE GYNVYDGDEQ NEVT
