CRUM1_MOUSE
ID CRUM1_MOUSE Reviewed; 1405 AA.
AC Q8VHS2; B7ZC63; Q6ST50; Q71JF2; Q8BGR4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein crumbs homolog 1;
DE Flags: Precursor;
GN Name=Crb1;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Eye;
RX PubMed=11744384; DOI=10.1016/s0925-4773(01)00568-8;
RA den Hollander A.I., Ghiani M., de Kok Y.J.M., Wijnholds J., Ballabio A.,
RA Cremers F.P.M., Broccoli V.;
RT "Isolation of Crb1, a mouse homologue of Drosophila crumbs, and analysis of
RT its expression pattern in eye and brain.";
RL Mech. Dev. 110:203-207(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ICR; TISSUE=Skin;
RX PubMed=14684155; DOI=10.1016/j.bbrc.2003.11.122;
RA Watanabe T., Miyatani S., Katoh I., Kobayashi S., Ikawa Y.;
RT "Expression of a novel secretory form (Crb1s) of mouse Crumbs homologue
RT Crb1 in skin development.";
RL Biochem. Biophys. Res. Commun. 313:263-270(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ICR;
RA Chang C.-H., Fan S.-S.;
RT "Mouse Crumbs-2 in developing nervous system.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11850625; DOI=10.1038/nature721;
RA Pellikka M., Tanentzapf G., Pinto M., Smith C., McGlade C.J., Ready D.F.,
RA Tepass U.;
RT "Crumbs, the Drosophila homologue of human CRB1/RP12, is essential for
RT photoreceptor morphogenesis.";
RL Nature 416:143-149(2002).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISEASE.
RX PubMed=12915475; DOI=10.1093/hmg/ddg232;
RA Mehalow A.K., Kameya S., Smith R.S., Hawes N.L., Denegre J.M., Young J.A.,
RA Bechtold L., Haider N.B., Tepass U., Heckenlively J.R., Chang B.,
RA Naggert J.K., Nishina P.M.;
RT "CRB1 is essential for external limiting membrane integrity and
RT photoreceptor morphogenesis in the mammalian retina.";
RL Hum. Mol. Genet. 12:2179-2189(2003).
RN [9]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH MPDZ; MPP4 AND PALS1, AND TISSUE
RP SPECIFICITY.
RX PubMed=15316081; DOI=10.1242/jcs.01301;
RA van de Pavert S.A., Kantardzhieva A., Malysheva A., Meuleman J.,
RA Versteeg I., Levelt C., Klooster J., Geiger S., Seeliger M.W., Rashbass P.,
RA Le Bivic A., Wijnholds J.;
RT "Crumbs homologue 1 is required for maintenance of photoreceptor cell
RT polarization and adhesion during light exposure.";
RL J. Cell Sci. 117:4169-4177(2004).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=23001562; DOI=10.1093/hmg/dds398;
RA Alves C.H., Sanz A.S., Park B., Pellissier L.P., Tanimoto N., Beck S.C.,
RA Huber G., Murtaza M., Richard F., Sridevi Gurubaran I., Garcia Garrido M.,
RA Levelt C.N., Rashbass P., Le Bivic A., Seeliger M.W., Wijnholds J.;
RT "Loss of CRB2 in the mouse retina mimics human retinitis pigmentosa due to
RT mutations in the CRB1 gene.";
RL Hum. Mol. Genet. 22:35-50(2013).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=26404741; DOI=10.1038/srep14504;
RA Paniagua A.E., Herranz-Martin S., Jimeno D., Jimeno A.M., Lopez-Benito S.,
RA Carlos Arevalo J., Velasco A., Aijon J., Lillo C.;
RT "CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment
RT Epithelium.";
RL Sci. Rep. 5:14504-14504(2015).
CC -!- FUNCTION: Plays a role in photoreceptor morphogenesis in the retina
CC (PubMed:12915475). May maintain cell polarization and adhesion
CC (PubMed:15316081). {ECO:0000269|PubMed:12915475,
CC ECO:0000269|PubMed:15316081}.
CC -!- FUNCTION: [Isoform 3]: May play a role in epidermal tissue
CC morphogenesis (PubMed:14684155). May function in cell attachment for
CC stratified epithelial organization (PubMed:14684155).
CC {ECO:0000269|PubMed:14684155}.
CC -!- SUBUNIT: Component of a complex composed of PALS1, CRB1 and EPB41L5 (By
CC similarity). Within the complex, interacts (via intracellular domain)
CC with PALS1 and EPB41L5 (via FERM domain) (By similarity). Forms a
CC complex with MPP4 and PALS1 (PubMed:15316081). Interacts with
CC MPDZ/MUPP1 and MPP4 (PubMed:15316081). {ECO:0000250|UniProtKB:P82279,
CC ECO:0000269|PubMed:15316081}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Apical cell membrane
CC {ECO:0000269|PubMed:11850625}; Single-pass type I membrane protein
CC {ECO:0000255}. Secreted {ECO:0000305}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000269|PubMed:11850625}.
CC Photoreceptor inner segment {ECO:0000269|PubMed:11850625}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted
CC {ECO:0000269|PubMed:14684155}. Cytoplasm {ECO:0000269|PubMed:14684155}.
CC Cell junction, focal adhesion {ECO:0000269|PubMed:14684155}. Note=Found
CC in the cytoplasmic area of undifferentiated keratinocytes and
CC associated with the plasma membrane at the site of cell-cell contacts
CC and focal adhesion upon keratinocytes differentiation.
CC {ECO:0000269|PubMed:14684155}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8VHS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VHS2-2; Sequence=VSP_014731, VSP_014735, VSP_014736;
CC Name=3; Synonyms=Crb1s {ECO:0000303|PubMed:14684155};
CC IsoId=Q8VHS2-3; Sequence=VSP_014733, VSP_014734;
CC Name=4;
CC IsoId=Q8VHS2-4; Sequence=VSP_014730, VSP_014732, VSP_014733,
CC VSP_014734;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in the kidney, lung, stomach
CC and testis (PubMed:14684155). Expressed in the brain (PubMed:11744384,
CC PubMed:14684155). Expressed in the retina of the eye (PubMed:11744384,
CC PubMed:14684155, PubMed:26404741). Expressed in the outer nuclear
CC layer, photoreceptor layer and inner nuclear layer of the retina
CC (PubMed:11744384). Expressed in Mueller cell radial processes in the
CC inner nuclear layer, in apical processes sclerad to the external
CC limiting membrane, and in the subapical region, adjacent to the
CC adherens junction of retinal photoreceptors (PubMed:12915475,
CC PubMed:15316081). In the brain, expressed in the granular layer of the
CC cerebellum, the hippocampal dentate gyrus, the olfactory bulbs, the
CC subventricular region lining the telencephalic ventricles and the
CC rostral migratory stream (PubMed:11744384).
CC {ECO:0000269|PubMed:11744384, ECO:0000269|PubMed:12915475,
CC ECO:0000269|PubMed:14684155, ECO:0000269|PubMed:15316081,
CC ECO:0000269|PubMed:26404741}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Ubiquitously expressed.
CC {ECO:0000269|PubMed:14684155}.
CC -!- DEVELOPMENTAL STAGE: Primarily detected in the central nervous system
CC at 10.5 dpc, in the ventral part of the neural tube including the
CC ventral spinal cord, the ventral part of the mesencephalon, the
CC mammillary and the hypothalamic regions, the optic area and the zona
CC limitans intrathalamica (PubMed:11744384). Expressed by the V3
CC interneurons placed between the floor plate and the motorneurons all
CC along the spinal cord axis (PubMed:11744384). In late embryogenesis,
CC expressed mainly in ventral neural structures of the developing brain,
CC including the mammillary, tuberalis regions of the hypothalamus and the
CC preoptic area (PubMed:11744384). Starting from 12.5 dpc, also strongly
CC expressed in the neural area that gives rise to the dorsal thalamus
CC (PubMed:11744384). In the retina, expression starts at 11.5 dpc and is
CC enhanced at 12.5, 14.5 and 16.5 dpc (PubMed:11744384). Expressed in the
CC subapical region of the neuroepithelial layer of the retina at 17.5 dpc
CC (PubMed:23001562). In postnatal stages, abundant expression in
CC photoreceptors and also found in the inner nuclear layer and iris
CC (PubMed:11744384). {ECO:0000269|PubMed:11744384,
CC ECO:0000269|PubMed:23001562}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 3]: Expression first detected at 14 dpc,
CC expression is enhanced at 15 and 16 dpc during active proliferation of
CC epidermal cells, decreases after birth, but is maintained in adult skin
CC (PubMed:14684155). Detected in the skin basal cells at 16 dpc, it was
CC observed in upper layers after birth (at protein level)
CC (PubMed:14684155). {ECO:0000269|PubMed:14684155}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P82279}.
CC -!- DISEASE: Note=Defects in Crb1 are a cause of focal retinal dysplasia
CC and degeneration associated with a shortening of inner and outer
CC segments. Affected mice produce a secreted truncated protein that lacks
CC the single transmembrane and the intracellular domain, and develop
CC irregularities at the outer limiting membrane and loss of photoreceptor
CC cells. {ECO:0000269|PubMed:12915475}.
CC -!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}.
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DR EMBL; AF406641; AAL65131.1; -; mRNA.
DR EMBL; AY450552; AAR20495.1; -; mRNA.
DR EMBL; AF492496; AAQ06606.1; -; mRNA.
DR EMBL; AK044345; BAC31879.1; -; mRNA.
DR EMBL; AK044704; BAC32041.1; -; mRNA.
DR EMBL; AC116810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466520; EDL39531.1; -; Genomic_DNA.
DR CCDS; CCDS15336.1; -. [Q8VHS2-1]
DR RefSeq; NP_573502.2; NM_133239.2. [Q8VHS2-1]
DR AlphaFoldDB; Q8VHS2; -.
DR SMR; Q8VHS2; -.
DR BioGRID; 228439; 3.
DR CORUM; Q8VHS2; -.
DR STRING; 10090.ENSMUSP00000060769; -.
DR GlyGen; Q8VHS2; 11 sites.
DR iPTMnet; Q8VHS2; -.
DR PhosphoSitePlus; Q8VHS2; -.
DR PaxDb; Q8VHS2; -.
DR PRIDE; Q8VHS2; -.
DR ProteomicsDB; 285310; -. [Q8VHS2-1]
DR ProteomicsDB; 285311; -. [Q8VHS2-2]
DR Antibodypedia; 34478; 71 antibodies from 23 providers.
DR DNASU; 170788; -.
DR Ensembl; ENSMUST00000059825; ENSMUSP00000060769; ENSMUSG00000063681. [Q8VHS2-1]
DR Ensembl; ENSMUST00000196402; ENSMUSP00000142702; ENSMUSG00000063681. [Q8VHS2-3]
DR GeneID; 170788; -.
DR KEGG; mmu:170788; -.
DR UCSC; uc007cwc.1; mouse. [Q8VHS2-1]
DR UCSC; uc007cwe.1; mouse. [Q8VHS2-4]
DR UCSC; uc007cwf.1; mouse. [Q8VHS2-3]
DR CTD; 23418; -.
DR MGI; MGI:2136343; Crb1.
DR VEuPathDB; HostDB:ENSMUSG00000063681; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000155152; -.
DR HOGENOM; CLU_000827_2_2_1; -.
DR InParanoid; Q8VHS2; -.
DR OMA; NCTEFQG; -.
DR OrthoDB; 111153at2759; -.
DR PhylomeDB; Q8VHS2; -.
DR TreeFam; TF316224; -.
DR BioGRID-ORCS; 170788; 1 hit in 70 CRISPR screens.
DR PRO; PR:Q8VHS2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VHS2; protein.
DR Bgee; ENSMUSG00000063681; Expressed in retinal neural layer and 88 other tissues.
DR ExpressionAtlas; Q8VHS2; baseline and differential.
DR Genevisible; Q8VHS2; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0097386; C:glial cell projection; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035003; C:subapical complex; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:MGI.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:MGI.
DR GO; GO:0061159; P:establishment of bipolar cell polarity involved in cell morphogenesis; IMP:MGI.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IMP:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:MGI.
DR GO; GO:0007009; P:plasma membrane organization; IMP:MGI.
DR GO; GO:0060060; P:post-embryonic retina morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0010842; P:retina layer formation; IMP:MGI.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd00110; LamG; 3.
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; 12.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00179; EGF_CA; 16.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; SSF49899; 3.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 17.
DR PROSITE; PS01187; EGF_CA; 6.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell junction; Cell membrane;
KW Cell projection; Cytoplasm; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1405
FT /note="Protein crumbs homolog 1"
FT /id="PRO_0000007501"
FT TOPO_DOM 28..1339
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1340..1360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1361..1405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..67
FT /note="EGF-like 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 69..107
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 109..145
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 147..183
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 185..221
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 223..259
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 261..298
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 300..336
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 338..394
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 396..438
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 440..480
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 482..669
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 671..707
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 713..884
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 886..922
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 923..959
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 950..1136
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1138..1174
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1176..1211
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1213..1249
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1254..1294
FT /note="EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1296..1332
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..45
FT /evidence="ECO:0000250"
FT DISULFID 39..54
FT /evidence="ECO:0000250"
FT DISULFID 55..66
FT /evidence="ECO:0000250"
FT DISULFID 73..84
FT /evidence="ECO:0000250"
FT DISULFID 78..95
FT /evidence="ECO:0000250"
FT DISULFID 97..106
FT /evidence="ECO:0000250"
FT DISULFID 113..124
FT /evidence="ECO:0000250"
FT DISULFID 118..133
FT /evidence="ECO:0000250"
FT DISULFID 135..144
FT /evidence="ECO:0000250"
FT DISULFID 151..162
FT /evidence="ECO:0000250"
FT DISULFID 156..171
FT /evidence="ECO:0000250"
FT DISULFID 173..182
FT /evidence="ECO:0000250"
FT DISULFID 189..200
FT /evidence="ECO:0000250"
FT DISULFID 194..209
FT /evidence="ECO:0000250"
FT DISULFID 211..220
FT /evidence="ECO:0000250"
FT DISULFID 227..238
FT /evidence="ECO:0000250"
FT DISULFID 232..247
FT /evidence="ECO:0000250"
FT DISULFID 249..258
FT /evidence="ECO:0000250"
FT DISULFID 265..276
FT /evidence="ECO:0000250"
FT DISULFID 270..285
FT /evidence="ECO:0000250"
FT DISULFID 287..297
FT /evidence="ECO:0000250"
FT DISULFID 304..315
FT /evidence="ECO:0000250"
FT DISULFID 309..324
FT /evidence="ECO:0000250"
FT DISULFID 326..335
FT /evidence="ECO:0000250"
FT DISULFID 342..353
FT /evidence="ECO:0000250"
FT DISULFID 347..382
FT /evidence="ECO:0000250"
FT DISULFID 384..393
FT /evidence="ECO:0000250"
FT DISULFID 400..411
FT /evidence="ECO:0000250"
FT DISULFID 405..420
FT /evidence="ECO:0000250"
FT DISULFID 422..437
FT /evidence="ECO:0000250"
FT DISULFID 444..455
FT /evidence="ECO:0000250"
FT DISULFID 449..468
FT /evidence="ECO:0000250"
FT DISULFID 470..479
FT /evidence="ECO:0000250"
FT DISULFID 641..669
FT /evidence="ECO:0000250"
FT DISULFID 675..686
FT /evidence="ECO:0000250"
FT DISULFID 680..695
FT /evidence="ECO:0000250"
FT DISULFID 697..706
FT /evidence="ECO:0000250"
FT DISULFID 850..884
FT /evidence="ECO:0000250"
FT DISULFID 890..901
FT /evidence="ECO:0000250"
FT DISULFID 895..910
FT /evidence="ECO:0000250"
FT DISULFID 912..921
FT /evidence="ECO:0000250"
FT DISULFID 927..938
FT /evidence="ECO:0000250"
FT DISULFID 932..947
FT /evidence="ECO:0000250"
FT DISULFID 1095..1136
FT /evidence="ECO:0000250"
FT DISULFID 1142..1153
FT /evidence="ECO:0000250"
FT DISULFID 1147..1162
FT /evidence="ECO:0000250"
FT DISULFID 1164..1173
FT /evidence="ECO:0000250"
FT DISULFID 1180..1190
FT /evidence="ECO:0000250"
FT DISULFID 1185..1199
FT /evidence="ECO:0000250"
FT DISULFID 1201..1210
FT /evidence="ECO:0000250"
FT DISULFID 1217..1228
FT /evidence="ECO:0000250"
FT DISULFID 1222..1237
FT /evidence="ECO:0000250"
FT DISULFID 1239..1248
FT /evidence="ECO:0000250"
FT DISULFID 1258..1273
FT /evidence="ECO:0000250"
FT DISULFID 1267..1282
FT /evidence="ECO:0000250"
FT DISULFID 1284..1293
FT /evidence="ECO:0000250"
FT DISULFID 1300..1311
FT /evidence="ECO:0000250"
FT DISULFID 1305..1320
FT /evidence="ECO:0000250"
FT DISULFID 1322..1331
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..372
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014730"
FT VAR_SEQ 329..389
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_014731"
FT VAR_SEQ 373..389
FT /note="SYVGASGYVCICQPGFT -> MFGHKTQGFHILMAVLI (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014732"
FT VAR_SEQ 709..761
FT /note="EYVAGRFGQDDSTGYAAFSVNDNYGQNFSLSMFVRTRQPLGLLLALENSTYQ
FT Y -> GERSGVPQSAVPLSRAISNHPGCRPLLGNIRTPQDLCWYLFTNEIKWHSHDMY
FT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14684155,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_014733"
FT VAR_SEQ 762..1405
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14684155,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_014734"
FT VAR_SEQ 1298..1376
FT /note="NECASDPCINGGLCRDLVNRFLCICDVAFAGERCELDLADDRLLGIFTAVGS
FT GTLALFFILLLAGVASLIASNKRATQG -> EASVPPIPASMEDCAGTWSTGSYASVMW
FT PSLGERCELDVSGLSFYVSLLLWQNLFQLLSYLVLHMNDEPVVEWGAQENY (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_014735"
FT VAR_SEQ 1377..1405
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_014736"
FT CONFLICT 46
FT /note="K -> E (in Ref. 1; AAL65131 and 2; AAR20495)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="H -> L (in Ref. 1; AAL65131)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="E -> K (in Ref. 2; AAR20495)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="S -> T (in Ref. 2; AAR20495)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="S -> N (in Ref. 2; AAR20495)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="S -> T (in Ref. 2; AAR20495)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="N -> S (in Ref. 1; AAL65131)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="Missing (in Ref. 2; AAR20495)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="L -> W (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="C -> G (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="I -> M (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="T -> P (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="T -> A (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="D -> DD (in Ref. 2; AAR20495)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="F -> L (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="R -> H (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="P -> L (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 886
FT /note="G -> R (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 900..902
FT /note="VCH -> ACR (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="P -> S (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="H -> Q (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062
FT /note="I -> V (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
FT CONFLICT 1275
FT /note="M -> V (in Ref. 3; AAQ06606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1405 AA; 153350 MW; FE1ECCB17529797B CRC64;
MKLKRTAYLL FLYLSSSLLI CIKNSFCNKN NTRCLSGPCQ NNSTCKHFPQ DNNCCLDTAN
NLDKDCEDLK DPCFSSPCQG IATCVKIPGE GNFLCQCPPG YSGLNCETAT NSCGGNLCQH
GGTCRKDPEH PVCICPPGYA GRFCETDHNE CASSPCHNGA MCQDGINGYS CFCVPGYQGR
HCDLEVDECV SDPCKNEAVC LNEIGRYTCV CPQEFSGVNC ELEIDECRSQ PCLHGATCQD
APGGYSCDCA PGFLGEHCEL SVNECESQPC LHGGLCVDGR NSYHCDCTGS GFTGMHCESL
IPLCWSKPCH NDATCEDTVD SYICHCRPGY TGALCETDIN ECSSNPCQFW GECVELSSEG
LYGNTAGLPS SFSYVGASGY VCICQPGFTG IHCEEDVDEC LLHPCLNGGT CENLPGNYAC
HCPFDDTSRT FYGGENCSEI LLGCTHHQCL NNGKCIPHFQ NGQHGFTCQC LSGYAGPLCE
TVTTLSFGSN GFLWVTSGSH TGIGPECNIS LRFHTVQPNA LLLIRGNKDV SMKLELLNGC
VHLSIEVWNQ LKVLLSISHN TSDGEWHFVE VTIAETLTLA LVGGSCKEKC TTKSSVPVEN
HQSICALQDS FLGGLPMGTA NNSVSVLNIY NVPSTPSFVG CLQDIRFDLN HITLENVSSG
LSSNVKAGCL GKDWCESQPC QNRGRCINLW QGYQCECDRP YTGSNCLKEY VAGRFGQDDS
TGYAAFSVND NYGQNFSLSM FVRTRQPLGL LLALENSTYQ YVSVWLEHGS LALQTPGSPK
FMVNFFLSDG NVHLISLRIK PNEIELYQSS QNLGFISVPT WTIRRGDVIF IGGLPDREKT
EVYGGFFKGC VQDVRLNSQT LEFFPNSTNN AYDDPILVNV TQGCPGDNTC KSNPCHNGGV
CHSLWDDFSC SCPTNTAGRA CEQVQWCQLS PCPPTAECQL LPQGFECIAN AVFSGLSREI
LFRSNGNITR ELTNITFAFR THDTNVMILH AEKEPEFLNI SIQDARLFFQ LRSGNSFYTL
HLMGSQLVND GTWHQVTFSM IDPVAQTSRW QMEVNDQTPF VISEVATGSL NFLKDNTDIY
VGDQSVDNPK GLQGCLSTIE IGGIYLSYFE NLHGFPGKPQ EEQFLKVSTN MVLTGCLPSN
ACHSSPCLHG GNCEDSYSSY RCACLSGWSG THCEINIDEC FSSPCIHGNC SDGVAAYHCR
CEPGYTGVNC EVDVDNCKSH QCANGATCVP EAHGYSCLCF GNFTGRFCRH SRLPSTVCGN
EKRNFTCYNG GSCSMFQEDW QCMCWPGFTG EWCEEDINEC ASDPCINGGL CRDLVNRFLC
ICDVAFAGER CELDLADDRL LGIFTAVGSG TLALFFILLL AGVASLIASN KRATQGTYSP
SGQEKAGPRV EMWIRMPPPA LERLI
