A0A2K5V015 · EYS_MACFA
- ProteinProtein eyes shut homolog
- GeneEYS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids3165 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Required to maintain the integrity of photoreceptor cells (By similarity).
Specifically required for normal morphology of the photoreceptor ciliary pocket, and might thus facilitate protein trafficking between the photoreceptor inner and outer segments via the transition zone (By similarity).
Specifically required for normal morphology of the photoreceptor ciliary pocket, and might thus facilitate protein trafficking between the photoreceptor inner and outer segments via the transition zone (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Cellular Component | interphotoreceptor matrix | |
Cellular Component | photoreceptor outer segment | |
Molecular Function | calcium ion binding | |
Biological Process | visual perception |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameProtein eyes shut homolog
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionA0A2K5V015
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to discrete puncta at, or adjacent to, the photoreceptor connecting cilium (PubMed:27737822).
Highly expressed in cone photoreceptor outer segments (PubMed:27737822, PubMed:27846257).
Weakly expressed in rod photoreceptor outer segments (PubMed:27737822).
May localize to the cilium axoneme (PubMed:27846257).
May also be secreted into the interphotoreceptor extracellular matrix (PubMed:27737822).
Highly expressed in cone photoreceptor outer segments (PubMed:27737822, PubMed:27846257).
Weakly expressed in rod photoreceptor outer segments (PubMed:27737822).
May localize to the cilium axoneme (PubMed:27846257).
May also be secreted into the interphotoreceptor extracellular matrix (PubMed:27737822).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MTDKSIIILSLMVFHSSFING | ||||||
Chain | PRO_5014416866 | 22-3165 | Protein eyes shut homolog | |||
Sequence: KTCRRELVEEWHPQPSSHVVNWTLTENICLDYYRDCWFLGVNTKIDTSGNQVVPQICPLQIQLGDILVISSEPSLQFPEINLMNVSETSFIGCVQNTTTEDQLLFGCRLKGMHTVNSKWLSVGTHYFITVMASGPSPCPLGLRLNVTVKQQFCQESLSSEFCSGHGKCLSEAWSKTYSCHCQPPFSGKYCQELDACSFKPCKNDGSCINKRGNWDEQGYECVCHPPFTGKNCSEIIVQCQPHVCFHGNCSNITSNSFICECDEQFSGPFCEVSTKPCVSLLCWKRGICPNSSSAYTYECPKGPSSQNGETDVSECSLILCENGTDGIKISNDVMCICSPIFTDLLCKSFQTSCESFPLKNNATFKKCEKDYHCSCMSGFTGKNCEKVIDHCKLLSINCLNEEWCFNIIGRFKYVCIPGCTKNPFWFLKNVHLIHLHPCYYGITFHGICQDKGPAHFEYVWQLGFTGSEGEKCQGVIDAYFFLTANCTEDAIYVNNPEDNNSSCSFPCEGTKEICANGCSCLSEEDNQEYRYLCFLRWTSNMYLENITDDQENKSQHEAICEDEINRPRCSCSLSYIGRLCVVNVDYCLGNQSISVHGLCLALSHNCNCSDLQKYEGNICEIDIEDCKSVSCKNGTTSIHLRGYFFYKCVPGFKGTRCEIDLDECALHPCKSGATCIDQPGNYFCQCGPPFKVVDGFSCLCNPGYVGTRCEQNIDNCILNAFEHNSTYKDLHLSYQCVCLSGWEGNFCEQESNECKMNPCKNNSTCTDLYKSYRCECTSGWTGQNCSEEINECDSDPCMNGGLCHESTIPGQFVCLCPPLYTGQFCHQRYNPCDLLNNPCRNNSTCLALVDGNQHCICREEFEGKHCEIDVKECLFLSCQDYGDCEDMVNNFRCICRPGFSGSLCEIEINECSSEPCKNNGTCVDLTNRFFCNCEPGYHGPFCELEVNKCKISPCLDEENCVYRTDRYNCLCAPGYTGINCEINLDECLSEPCLHDGVCIDGINHYTCDCKSGFFGTHCETNANDCLSNPCLHGRCTEPINEYPCSCDADGTSIQCKIKINDCTSMPCMNEGFCQKSAHGFTCICPRGYTGAYCEKSIDNCAEPELNSVICLNGGICVDGPGHTFDCRCLPGFSGQFCEININECSSSPCLHGANCEDHINGYVCKCQPGWSGHHCEKELECVPNSCVHQLCMENEPGSTCLCTPGFMTCSIGLLCGDEIRRITCLTPSFQRTDPISTQTHTVPPSETLVSSFPSIKATRIPTIMDTYPVDQGPKQTGIVKHDILPTTGLATLRISTPLKSYLLEELIVTRELSAKHSLLSSTDVSSSPFLNFGIHDPAQIVQDKTSVSHMRIRTSAATLGFFFPDRRARTSFIRSSLMSDFIFPTQSLLFENYQTVASSATPTTSVIRSIPGADIELNRHSLLSRGFLLTAASISATPVVSRGAQEDIKEYSAVSLISRREHWRSLISSMSPIFPAKKIISKQVTILNSSALHRFGTKAFIPSEYQAITEASSNQRLTNIKSQAADSLRELSQTCATCSMTEIKSSHEFSDQVLHSKQSHFYETFWMNSAILASWYALMGAQTITSGHSFSSATEITPSVAFTEVPSLFPSKKSAKRTILSSSLEESITLSSNLDVNLCLHKTCLSIVPSQTISSDLMNSDLTSELTTDELSVSENILKLLKIRQYGITTGPTEVLNQDSLLDMEKSKGSHTPFKLHPSDSSLDLELNLRSYPDVTLKTYSEITLANDLKNNLPPLTGSVPDFSEVTTNVAFYTVSATPALPIQTSSSMSVITPDWPYFIDYMTSLNKEVKTYSEWSKWELQPSVQYQEFPTASWHLPFTRSLTLSSLESIVAPQQLMISDFSCVCYYGDSYLEFQNVVLNPQNNISLEFQTFSSYGLLLYVKQDSNLVDGFFIQLSIENGTLKYHFYCPGEAKFKSINTAIRVDDGQKYTLLIRQELDPCKAELTILGRNTQTCESINHVLGKPLPKSGSVFIGGFPDLRGKIQMPVPVKNFTGCIEVIEINNWRSFIPSKAVRNYHINNCRSQGLMLSPTASFVDASDVTQGVDAMWTSVSPSVAAPSVCQEDVCHNGGTCRPIFLSSGIVSFQCDCPLHFTGRFCEKDAGLFFPSFSGNSYLELPFLNFVLEKEHNRTVTIYLTIKTNSLNGTILYSNGNNFGKQFLHLFLVEGKPSVKYGCGNSQNILTVSANYSINTNAFTPITVRHTMPIGSPGVVCMIEMTADGKPPVQKKDTEISHASQVYFESMFLGHIPENVQIHKKAGSVYGFRGCILDLQINNKEFFIIDEARRGKNIENCHVPWCAHHLCRNNGTCLSDSENLFCECPRLYSGKLCQFASCENNPCGNGATCVPKSGTDIICLCPYGRSGPLCTDAINITQPRFSGTDAFGYTSFLAYSRISDISFHYEFHLKFQLANNHSALQNNLIFFTGQKGHGLNGDDFLAVGLLNGSVVYSYNLGSGIASIRSDPLNLSLGVHTVHLGKFFQEGWLKVDDHKNKSIIAPGRLVGLNVFSQFYVGGYSEYTPDLLPNGADFKNGFQGCIFTLQVRTEKDGHFRGLGNPEGHPNAGRSVGQCHASPCSLMKCGNGGTCIESGTSVYCNCTTRWKGAFCTETVSICDPEHDPPHHCSRGATCISLPHGYTCFCPLGTTGIYCEQALILTVILEKPKPAEWKVKKEALSISDPSFRSSELSWMSFASFHVRKKTHIQLQFQPLAADGILFYAAQHLKAQSGDFLCISLVNGSVQLRYNLGDRTIILETLQKVTINGSTWHIIKAGRVGAEGYLDLDGINVTEKASTKMSSLDTNTDFYIGGVSSLNLVNPMAIENEPVGFHGCIRQVIINYQELQLTEFGAKGGSNVGDCDGTACGYNTCRNGGECRVNGTTFSCRCLPDWAGNICNQSAYCLNNLCLHQSLCIPDQSFSYSCLCTLGWVGRYCENKTSFTTAKFMGNSYIKYIDPNYRMRNLQFTTISLNFSTTKTEGLIIWMGIAQNEENDFLAIGLHNQTLKIAVNLGERISVPMSYNNGTFCCNKWHHVIVIQNQTLIKAYVNNSLILSEDIDPHKNFVALNYEGICYLGGFEYGRKVNIVTQEIFKTNFVGKIKDVVFFQDPKKIELIKLEGYNVYDGDEQNEVT | ||||||
Glycosylation | 42 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 105 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 117 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 166 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 174↔189 | |||||
Sequence: CQESLSSEFCSGHGKC | ||||||
Disulfide bond | 183↔200 | |||||
Sequence: CSGHGKCLSEAWSKTYSC | ||||||
Disulfide bond | 202↔211 | |||||
Sequence: CQPPFSGKYC | ||||||
Disulfide bond | 217↔228 | |||||
Sequence: CSFKPCKNDGSC | ||||||
Disulfide bond | 222↔242 | |||||
Sequence: CKNDGSCINKRGNWDEQGYEC | ||||||
Disulfide bond | 244↔253 | |||||
Sequence: CHPPFTGKNC | ||||||
Glycosylation | 252 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 260↔270 | |||||
Sequence: CQPHVCFHGNC | ||||||
Disulfide bond | 265↔280 | |||||
Sequence: CFHGNCSNITSNSFIC | ||||||
Glycosylation | 269 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 272 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 282↔291 | |||||
Sequence: CDEQFSGPFC | ||||||
Glycosylation | 311 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 341↔356 | |||||
Sequence: CENGTDGIKISNDVMC | ||||||
Glycosylation | 343 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 358↔367 | |||||
Sequence: CSPIFTDLLC | ||||||
Glycosylation | 382 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 396↔405 | |||||
Sequence: CMSGFTGKNC | ||||||
Glycosylation | 506 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 520 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 521 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 566 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 573 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 592↔601 | |||||
Sequence: CSLSYIGRLC | ||||||
Disulfide bond | 608↔620 | |||||
Sequence: CLGNQSISVHGLC | ||||||
Glycosylation | 611 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 628 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 629↔640 | |||||
Sequence: CSDLQKYEGNIC | ||||||
Glycosylation | 654 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 669↔678 | |||||
Sequence: CVPGFKGTRC | ||||||
Disulfide bond | 685↔696 | |||||
Sequence: CALHPCKSGATC | ||||||
Disulfide bond | 690↔705 | |||||
Sequence: CKSGATCIDQPGNYFC | ||||||
Disulfide bond | 707↔719 | |||||
Sequence: CGPPFKVVDGFSC | ||||||
Glycosylation | 745 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 759↔768 | |||||
Sequence: CLSGWEGNFC | ||||||
Disulfide bond | 775↔786 | |||||
Sequence: CKMNPCKNNSTC | ||||||
Disulfide bond | 780↔795 | |||||
Sequence: CKNNSTCTDLYKSYRC | ||||||
Glycosylation | 782 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 783 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 797↔806 | |||||
Sequence: CTSGWTGQNC | ||||||
Glycosylation | 805 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 813↔824 | |||||
Sequence: CDSDPCMNGGLC | ||||||
Disulfide bond | 818↔835 | |||||
Sequence: CMNGGLCHESTIPGQFVC | ||||||
Disulfide bond | 837↔846 | |||||
Sequence: CPPLYTGQFC | ||||||
Disulfide bond | 853↔866 | |||||
Sequence: CDLLNNPCRNNSTC | ||||||
Disulfide bond | 860↔876 | |||||
Sequence: CRNNSTCLALVDGNQHC | ||||||
Glycosylation | 862 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 863 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 878↔887 | |||||
Sequence: CREEFEGKHC | ||||||
Disulfide bond | 894↔905 | |||||
Sequence: CLFLSCQDYGDC | ||||||
Disulfide bond | 899↔914 | |||||
Sequence: CQDYGDCEDMVNNFRC | ||||||
Disulfide bond | 916↔925 | |||||
Sequence: CRPGFSGSLC | ||||||
Disulfide bond | 932↔943 | |||||
Sequence: CSSEPCKNNGTC | ||||||
Disulfide bond | 937↔952 | |||||
Sequence: CKNNGTCVDLTNRFFC | ||||||
Glycosylation | 940 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 954↔963 | |||||
Sequence: CEPGYHGPFC | ||||||
Disulfide bond | 970↔981 | |||||
Sequence: CKISPCLDEENC | ||||||
Disulfide bond | 975↔990 | |||||
Sequence: CLDEENCVYRTDRYNC | ||||||
Disulfide bond | 992↔1001 | |||||
Sequence: CAPGYTGINC | ||||||
Disulfide bond | 1008↔1019 | |||||
Sequence: CLSEPCLHDGVC | ||||||
Disulfide bond | 1013↔1028 | |||||
Sequence: CLHDGVCIDGINHYTC | ||||||
Disulfide bond | 1030↔1039 | |||||
Sequence: CKSGFFGTHC | ||||||
Disulfide bond | 1046↔1056 | |||||
Sequence: CLSNPCLHGRC | ||||||
Disulfide bond | 1051↔1065 | |||||
Sequence: CLHGRCTEPINEYPC | ||||||
Disulfide bond | 1067↔1076 | |||||
Sequence: CDADGTSIQC | ||||||
Disulfide bond | 1083↔1094 | |||||
Sequence: CTSMPCMNEGFC | ||||||
Disulfide bond | 1088↔1103 | |||||
Sequence: CMNEGFCQKSAHGFTC | ||||||
Disulfide bond | 1105↔1114 | |||||
Sequence: CPRGYTGAYC | ||||||
Disulfide bond | 1121↔1137 | |||||
Sequence: CAEPELNSVICLNGGIC | ||||||
Disulfide bond | 1131↔1147 | |||||
Sequence: CLNGGICVDGPGHTFDC | ||||||
Disulfide bond | 1149↔1158 | |||||
Sequence: CLPGFSGQFC | ||||||
Disulfide bond | 1165↔1176 | |||||
Sequence: CSSSPCLHGANC | ||||||
Disulfide bond | 1170↔1185 | |||||
Sequence: CLHGANCEDHINGYVC | ||||||
Disulfide bond | 1187↔1196 | |||||
Sequence: CQPGWSGHHC | ||||||
Glycosylation | 1509 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1906 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1941 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2033 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2037↔2063 | |||||
Sequence: CIEVIEINNWRSFIPSKAVRNYHINNC | ||||||
Disulfide bond | 2103↔2114 | |||||
Sequence: CQEDVCHNGGTC | ||||||
Disulfide bond | 2108↔2128 | |||||
Sequence: CHNGGTCRPIFLSSGIVSFQC | ||||||
Disulfide bond | 2130↔2139 | |||||
Sequence: CPLHFTGRFC | ||||||
Glycosylation | 2170 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2185 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2228 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2308↔2339 | |||||
Sequence: CILDLQINNKEFFIIDEARRGKNIENCHVPWC | ||||||
Disulfide bond | 2339↔2350 | |||||
Sequence: CAHHLCRNNGTC | ||||||
Disulfide bond | 2344↔2359 | |||||
Sequence: CRNNGTCLSDSENLFC | ||||||
Glycosylation | 2347 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2375↔2386 | |||||
Sequence: CENNPCGNGATC | ||||||
Disulfide bond | 2380↔2396 | |||||
Sequence: CGNGATCVPKSGTDIIC | ||||||
Disulfide bond | 2398↔2407 | |||||
Sequence: CPYGRSGPLC | ||||||
Glycosylation | 2412 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2453 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2484 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2506 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2532 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2576↔2609 | |||||
Sequence: CIFTLQVRTEKDGHFRGLGNPEGHPNAGRSVGQC | ||||||
Disulfide bond | 2614↔2625 | |||||
Sequence: CSLMKCGNGGTC | ||||||
Disulfide bond | 2619↔2634 | |||||
Sequence: CGNGGTCIESGTSVYC | ||||||
Glycosylation | 2635 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2636↔2645 | |||||
Sequence: CTTRWKGAFC | ||||||
Disulfide bond | 2652↔2668 | |||||
Sequence: CDPEHDPPHHCSRGATC | ||||||
Disulfide bond | 2662↔2677 | |||||
Sequence: CSRGATCISLPHGYTC | ||||||
Disulfide bond | 2679↔2688 | |||||
Sequence: CPLGTTGIYC | ||||||
Glycosylation | 2775 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2800 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2824 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2868↔2895 | |||||
Sequence: CIRQVIINYQELQLTEFGAKGGSNVGDC | ||||||
Disulfide bond | 2900↔2911 | |||||
Sequence: CGYNTCRNGGEC | ||||||
Disulfide bond | 2905↔2920 | |||||
Sequence: CRNGGECRVNGTTFSC | ||||||
Glycosylation | 2914 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2922↔2931 | |||||
Sequence: CLPDWAGNIC | ||||||
Glycosylation | 2932 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2937↔2948 | |||||
Sequence: CLNNLCLHQSLC | ||||||
Disulfide bond | 2942↔2958 | |||||
Sequence: CLHQSLCIPDQSFSYSC | ||||||
Disulfide bond | 2960↔2969 | |||||
Sequence: CTLGWVGRYC | ||||||
Glycosylation | 2971 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3006 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3036 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3057 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3073 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3082 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Expressed in retina (at protein level).
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 170-212 | EGF-like 1 | ||||
Sequence: KQQFCQESLSSEFCSGHGKCLSEAWSKTYSCHCQPPFSGKYCQ | ||||||
Domain | 213-254 | EGF-like 2 | ||||
Sequence: ELDACSFKPCKNDGSCINKRGNWDEQGYECVCHPPFTGKNCS | ||||||
Domain | 256-292 | EGF-like 3 | ||||
Sequence: IIVQCQPHVCFHGNCSNITSNSFICECDEQFSGPFCE | ||||||
Domain | 332-368 | EGF-like 4 | ||||
Sequence: DVSECSLILCENGTDGIKISNDVMCICSPIFTDLLCK | ||||||
Domain | 370-406 | EGF-like 5 | ||||
Sequence: FQTSCESFPLKNNATFKKCEKDYHCSCMSGFTGKNCE | ||||||
Domain | 566-602 | EGF-like 6 | ||||
Sequence: NITDDQENKSQHEAICEDEINRPRCSCSLSYIGRLCV | ||||||
Domain | 604-641 | EGF-like 7 | ||||
Sequence: NVDYCLGNQSISVHGLCLALSHNCNCSDLQKYEGNICE | ||||||
Domain | 643-679 | EGF-like 8 | ||||
Sequence: DIEDCKSVSCKNGTTSIHLRGYFFYKCVPGFKGTRCE | ||||||
Domain | 681-720 | EGF-like 9; calcium-binding | ||||
Sequence: DLDECALHPCKSGATCIDQPGNYFCQCGPPFKVVDGFSCL | ||||||
Domain | 733-769 | EGF-like 10 | ||||
Sequence: NIDNCILNAFEHNSTYKDLHLSYQCVCLSGWEGNFCE | ||||||
Domain | 771-807 | EGF-like 11; calcium-binding | ||||
Sequence: ESNECKMNPCKNNSTCTDLYKSYRCECTSGWTGQNCS | ||||||
Domain | 809-847 | EGF-like 12 | ||||
Sequence: EINECDSDPCMNGGLCHESTIPGQFVCLCPPLYTGQFCH | ||||||
Domain | 849-888 | EGF-like 13 | ||||
Sequence: RYNPCDLLNNPCRNNSTCLALVDGNQHCICREEFEGKHCE | ||||||
Domain | 890-926 | EGF-like 14 | ||||
Sequence: DVKECLFLSCQDYGDCEDMVNNFRCICRPGFSGSLCE | ||||||
Domain | 928-964 | EGF-like 15; calcium-binding | ||||
Sequence: EINECSSEPCKNNGTCVDLTNRFFCNCEPGYHGPFCE | ||||||
Domain | 966-1002 | EGF-like 16 | ||||
Sequence: EVNKCKISPCLDEENCVYRTDRYNCLCAPGYTGINCE | ||||||
Domain | 1004-1040 | EGF-like 17; calcium-binding | ||||
Sequence: NLDECLSEPCLHDGVCIDGINHYTCDCKSGFFGTHCE | ||||||
Domain | 1042-1077 | EGF-like 18 | ||||
Sequence: NANDCLSNPCLHGRCTEPINEYPCSCDADGTSIQCK | ||||||
Domain | 1079-1115 | EGF-like 19 | ||||
Sequence: KINDCTSMPCMNEGFCQKSAHGFTCICPRGYTGAYCE | ||||||
Domain | 1117-1159 | EGF-like 20 | ||||
Sequence: SIDNCAEPELNSVICLNGGICVDGPGHTFDCRCLPGFSGQFCE | ||||||
Domain | 1161-1197 | EGF-like 21; calcium-binding | ||||
Sequence: NINECSSSPCLHGANCEDHINGYVCKCQPGWSGHHCE | ||||||
Domain | 1883-2063 | Laminin G-like 1 | ||||
Sequence: FSCVCYYGDSYLEFQNVVLNPQNNISLEFQTFSSYGLLLYVKQDSNLVDGFFIQLSIENGTLKYHFYCPGEAKFKSINTAIRVDDGQKYTLLIRQELDPCKAELTILGRNTQTCESINHVLGKPLPKSGSVFIGGFPDLRGKIQMPVPVKNFTGCIEVIEINNWRSFIPSKAVRNYHINNC | ||||||
Domain | 2099-2140 | EGF-like 22 | ||||
Sequence: APSVCQEDVCHNGGTCRPIFLSSGIVSFQCDCPLHFTGRFCE | ||||||
Domain | 2145-2339 | Laminin G-like 2 | ||||
Sequence: LFFPSFSGNSYLELPFLNFVLEKEHNRTVTIYLTIKTNSLNGTILYSNGNNFGKQFLHLFLVEGKPSVKYGCGNSQNILTVSANYSINTNAFTPITVRHTMPIGSPGVVCMIEMTADGKPPVQKKDTEISHASQVYFESMFLGHIPENVQIHKKAGSVYGFRGCILDLQINNKEFFIIDEARRGKNIENCHVPWC | ||||||
Domain | 2335-2368 | EGF-like 23 | ||||
Sequence: HVPWCAHHLCRNNGTCLSDSENLFCECPRLYSGK | ||||||
Domain | 2371-2408 | EGF-like 24 | ||||
Sequence: QFASCENNPCGNGATCVPKSGTDIICLCPYGRSGPLCT | ||||||
Domain | 2419-2609 | Laminin G-like 3 | ||||
Sequence: SGTDAFGYTSFLAYSRISDISFHYEFHLKFQLANNHSALQNNLIFFTGQKGHGLNGDDFLAVGLLNGSVVYSYNLGSGIASIRSDPLNLSLGVHTVHLGKFFQEGWLKVDDHKNKSIIAPGRLVGLNVFSQFYVGGYSEYTPDLLPNGADFKNGFQGCIFTLQVRTEKDGHFRGLGNPEGHPNAGRSVGQC | ||||||
Domain | 2610-2646 | EGF-like 25 | ||||
Sequence: HASPCSLMKCGNGGTCIESGTSVYCNCTTRWKGAFCT | ||||||
Domain | 2648-2689 | EGF-like 26 | ||||
Sequence: TVSICDPEHDPPHHCSRGATCISLPHGYTCFCPLGTTGIYCE | ||||||
Domain | 2717-2895 | Laminin G-like 4 | ||||
Sequence: DPSFRSSELSWMSFASFHVRKKTHIQLQFQPLAADGILFYAAQHLKAQSGDFLCISLVNGSVQLRYNLGDRTIILETLQKVTINGSTWHIIKAGRVGAEGYLDLDGINVTEKASTKMSSLDTNTDFYIGGVSSLNLVNPMAIENEPVGFHGCIRQVIINYQELQLTEFGAKGGSNVGDC | ||||||
Domain | 2896-2932 | EGF-like 27 | ||||
Sequence: DGTACGYNTCRNGGECRVNGTTFSCRCLPDWAGNICN | ||||||
Domain | 2933-2970 | EGF-like 28 | ||||
Sequence: QSAYCLNNLCLHQSLCIPDQSFSYSCLCTLGWVGRYCE | ||||||
Domain | 2975-3165 | Laminin G-like 5 | ||||
Sequence: FTTAKFMGNSYIKYIDPNYRMRNLQFTTISLNFSTTKTEGLIIWMGIAQNEENDFLAIGLHNQTLKIAVNLGERISVPMSYNNGTFCCNKWHHVIVIQNQTLIKAYVNNSLILSEDIDPHKNFVALNYEGICYLGGFEYGRKVNIVTQEIFKTNFVGKIKDVVFFQDPKKIELIKLEGYNVYDGDEQNEVT |
Sequence similarities
Belongs to the EYS family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length3,165
- Mass (Da)351,050
- Last updated2018-03-28 v1
- Checksum8FE6949946E3435E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AQIA01051412 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AQIA01051413 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AQIA01051414 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AQIA01051415 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AQIA01051416 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AQIA01051417 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AQIA01051418 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AQIA01051419 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AQIA01051420 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AQIA01051421 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |