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Q8VHS2

- CRUM1_MOUSE

UniProt

Q8VHS2 - CRUM1_MOUSE

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Protein

Protein crumbs homolog 1

Gene

Crb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in photoreceptor morphogenesis in the retina. May maintain cell polarization and adhesion. Isoform 3 could play a role in epidermal tissue morphogenesis. May function in cell attachment for stratified epithelial organization.3 Publications

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. eye photoreceptor cell development Source: MGI
  2. membrane organization Source: MGI
  3. plasma membrane organization Source: MGI
Complete GO annotation...

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Protein crumbs homolog 1
Gene namesi
Name:Crb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2136343. Crb1.

Subcellular locationi

Isoform 1 : Membrane; Single-pass type I membrane protein
Note: In the retina, localizes to the Mueller cell radial processes in the inner nuclear layer and in apical processes sclerad to the external limiting membrane. Localizes to the subapical region, adjacent to the adherens junction of photoreceptors. Isoform 3 which is secreted is found in the cytoplasmic area of undifferentiated keratinocytes and associates with the plasma membrane at the site of cell-cell contacts and focal adhesion upon keratinocytes differentiation.

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. microvillus Source: MGI
  3. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in Crb1 are a cause of focal retinal dysplasia and degeneration associated with a shortening of inner and outer segments. Affected mice produce a secreted truncated protein that lacks the single transmembrane and the intracellular domain, and develop irregularities at the outer limiting membrane and loss of photoreceptor cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 14051378Protein crumbs homolog 1PRO_0000007501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 45By similarity
Disulfide bondi39 ↔ 54By similarity
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi55 ↔ 66By similarity
Disulfide bondi73 ↔ 84By similarity
Disulfide bondi78 ↔ 95By similarity
Disulfide bondi97 ↔ 106By similarity
Disulfide bondi113 ↔ 124By similarity
Disulfide bondi118 ↔ 133By similarity
Disulfide bondi135 ↔ 144By similarity
Disulfide bondi151 ↔ 162By similarity
Disulfide bondi156 ↔ 171By similarity
Disulfide bondi173 ↔ 182By similarity
Disulfide bondi189 ↔ 200By similarity
Disulfide bondi194 ↔ 209By similarity
Disulfide bondi211 ↔ 220By similarity
Disulfide bondi227 ↔ 238By similarity
Disulfide bondi232 ↔ 247By similarity
Disulfide bondi249 ↔ 258By similarity
Disulfide bondi265 ↔ 276By similarity
Disulfide bondi270 ↔ 285By similarity
Disulfide bondi287 ↔ 297By similarity
Disulfide bondi304 ↔ 315By similarity
Disulfide bondi309 ↔ 324By similarity
Disulfide bondi326 ↔ 335By similarity
Disulfide bondi342 ↔ 353By similarity
Disulfide bondi347 ↔ 382By similarity
Disulfide bondi384 ↔ 393By similarity
Disulfide bondi400 ↔ 411By similarity
Disulfide bondi405 ↔ 420By similarity
Disulfide bondi422 ↔ 437By similarity
Disulfide bondi444 ↔ 455By similarity
Disulfide bondi449 ↔ 468By similarity
Disulfide bondi470 ↔ 479By similarity
Glycosylationi560 – 5601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi641 ↔ 669By similarity
Glycosylationi656 – 6561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi675 ↔ 686By similarity
Disulfide bondi680 ↔ 695By similarity
Disulfide bondi697 ↔ 706By similarity
Glycosylationi756 – 7561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi850 ↔ 884By similarity
Glycosylationi879 – 8791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi890 ↔ 901By similarity
Disulfide bondi895 ↔ 910By similarity
Disulfide bondi912 ↔ 921By similarity
Disulfide bondi927 ↔ 938By similarity
Disulfide bondi932 ↔ 947By similarity
Glycosylationi967 – 9671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi974 – 9741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi999 – 9991N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1095 ↔ 1136By similarity
Disulfide bondi1142 ↔ 1153By similarity
Disulfide bondi1147 ↔ 1162By similarity
Disulfide bondi1164 ↔ 1173By similarity
Disulfide bondi1180 ↔ 1190By similarity
Disulfide bondi1185 ↔ 1199By similarity
Glycosylationi1189 – 11891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1201 ↔ 1210By similarity
Disulfide bondi1217 ↔ 1228By similarity
Disulfide bondi1222 ↔ 1237By similarity
Disulfide bondi1239 ↔ 1248By similarity
Glycosylationi1242 – 12421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1258 ↔ 1273By similarity
Glycosylationi1264 – 12641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1267 ↔ 1282By similarity
Disulfide bondi1284 ↔ 1293By similarity
Disulfide bondi1300 ↔ 1311By similarity
Disulfide bondi1305 ↔ 1320By similarity
Disulfide bondi1322 ↔ 1331By similarity

Post-translational modificationi

Glycosylated.Curated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8VHS2.

PTM databases

PhosphoSiteiQ8VHS2.

Expressioni

Tissue specificityi

Expressed exclusively in brain and proliferative retinoblasts of the eye. In the brain, expressed in the granular layer of the cerebellum, the hippocampal dentate gyrus, the olfactory bulbs, the subventricular region lining the telencephalic ventricles and the rostral migratory stream. Isoform 3 is ubiquitously expressed.2 Publications

Developmental stagei

Primarily detected in the central nervous system at E10.5, in the ventral part of the neural tube including the ventral spinal cord, the ventral part of the mesencephalon, the mammillary and the hypothalamic regions, the optic area and the zona limitans intrathalamica. Expressed by the V3 interneurons placed between the floor plate and the motorneurons all along the spinal cord axis. In late embryogenesis, expressed mainly in ventral neural structures of the developing brain, including the mammillary, tuberalis regions of the hypothalamus and the preoptic area. Starting from E12.5, also strongly expressed in the neural area that gives rise to the dorsal thalamus. In the retina, expression starts at E11.5 and is enhanced at E12.5, E14.5 and E16.5. In postnatal stages and in the adult eye, it is strongly expressed in photoreceptors and also found in inner nuclear layer and iris. Isoform 3 expression starts at E14, is enhanced at E15 and E16 during active proliferation of epidermal cells, decreases after birth but is maintained in adult skin. Detected in the skin basal cells at E16, it was observed in upper layers after birth (at protein level).2 Publications

Gene expression databases

BgeeiQ8VHS2.
CleanExiMM_CRB1.
ExpressionAtlasiQ8VHS2. baseline.
GenevestigatoriQ8VHS2.

Interactioni

Subunit structurei

In photoreceptor cells, forms a complex with MPDZ, MPP4 and MPP5.

Structurei

3D structure databases

ProteinModelPortaliQ8VHS2.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 13391312ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1361 – 140545CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1340 – 136021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 6738EGF-like 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Domaini69 – 10739EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini109 – 14537EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini147 – 18337EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini185 – 22137EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini223 – 25937EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini261 – 29838EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini300 – 33637EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini338 – 39457EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini396 – 43843EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini440 – 48041EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini482 – 669188Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini671 – 70737EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini713 – 884172Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini886 – 92237EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini923 – 95937EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini950 – 1136187Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini1138 – 117437EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Domaini1176 – 121136EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1213 – 124937EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini1254 – 129441EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini1296 – 133237EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the Crumbs protein family.Curated
Contains 19 EGF-like domains.PROSITE-ProRule annotation
Contains 3 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118786.
HOGENOMiHOG000230899.
HOVERGENiHBG080001.
InParanoidiQ8VHS2.
KOiK16681.
OMAiATFLNDS.
OrthoDBiEOG7KH9HX.
TreeFamiTF316224.

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00008. EGF. 11 hits.
PF12661. hEGF. 2 hits.
PF02210. Laminin_G_2. 3 hits.
[Graphical view]
SMARTiSM00181. EGF. 10 hits.
SM00179. EGF_CA. 7 hits.
SM00282. LamG. 3 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 3 hits.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 10 hits.
PS00022. EGF_1. 15 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 17 hits.
PS01187. EGF_CA. 6 hits.
PS50025. LAM_G_DOMAIN. 3 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8VHS2) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKLKRTAYLL FLYLSSSLLI CIKNSFCNKN NTRCLSGPCQ NNSTCKHFPQ
60 70 80 90 100
DNNCCLDTAN NLDKDCEDLK DPCFSSPCQG IATCVKIPGE GNFLCQCPPG
110 120 130 140 150
YSGLNCETAT NSCGGNLCQH GGTCRKDPEH PVCICPPGYA GRFCETDHNE
160 170 180 190 200
CASSPCHNGA MCQDGINGYS CFCVPGYQGR HCDLEVDECV SDPCKNEAVC
210 220 230 240 250
LNEIGRYTCV CPQEFSGVNC ELEIDECRSQ PCLHGATCQD APGGYSCDCA
260 270 280 290 300
PGFLGEHCEL SVNECESQPC LHGGLCVDGR NSYHCDCTGS GFTGMHCESL
310 320 330 340 350
IPLCWSKPCH NDATCEDTVD SYICHCRPGY TGALCETDIN ECSSNPCQFW
360 370 380 390 400
GECVELSSEG LYGNTAGLPS SFSYVGASGY VCICQPGFTG IHCEEDVDEC
410 420 430 440 450
LLHPCLNGGT CENLPGNYAC HCPFDDTSRT FYGGENCSEI LLGCTHHQCL
460 470 480 490 500
NNGKCIPHFQ NGQHGFTCQC LSGYAGPLCE TVTTLSFGSN GFLWVTSGSH
510 520 530 540 550
TGIGPECNIS LRFHTVQPNA LLLIRGNKDV SMKLELLNGC VHLSIEVWNQ
560 570 580 590 600
LKVLLSISHN TSDGEWHFVE VTIAETLTLA LVGGSCKEKC TTKSSVPVEN
610 620 630 640 650
HQSICALQDS FLGGLPMGTA NNSVSVLNIY NVPSTPSFVG CLQDIRFDLN
660 670 680 690 700
HITLENVSSG LSSNVKAGCL GKDWCESQPC QNRGRCINLW QGYQCECDRP
710 720 730 740 750
YTGSNCLKEY VAGRFGQDDS TGYAAFSVND NYGQNFSLSM FVRTRQPLGL
760 770 780 790 800
LLALENSTYQ YVSVWLEHGS LALQTPGSPK FMVNFFLSDG NVHLISLRIK
810 820 830 840 850
PNEIELYQSS QNLGFISVPT WTIRRGDVIF IGGLPDREKT EVYGGFFKGC
860 870 880 890 900
VQDVRLNSQT LEFFPNSTNN AYDDPILVNV TQGCPGDNTC KSNPCHNGGV
910 920 930 940 950
CHSLWDDFSC SCPTNTAGRA CEQVQWCQLS PCPPTAECQL LPQGFECIAN
960 970 980 990 1000
AVFSGLSREI LFRSNGNITR ELTNITFAFR THDTNVMILH AEKEPEFLNI
1010 1020 1030 1040 1050
SIQDARLFFQ LRSGNSFYTL HLMGSQLVND GTWHQVTFSM IDPVAQTSRW
1060 1070 1080 1090 1100
QMEVNDQTPF VISEVATGSL NFLKDNTDIY VGDQSVDNPK GLQGCLSTIE
1110 1120 1130 1140 1150
IGGIYLSYFE NLHGFPGKPQ EEQFLKVSTN MVLTGCLPSN ACHSSPCLHG
1160 1170 1180 1190 1200
GNCEDSYSSY RCACLSGWSG THCEINIDEC FSSPCIHGNC SDGVAAYHCR
1210 1220 1230 1240 1250
CEPGYTGVNC EVDVDNCKSH QCANGATCVP EAHGYSCLCF GNFTGRFCRH
1260 1270 1280 1290 1300
SRLPSTVCGN EKRNFTCYNG GSCSMFQEDW QCMCWPGFTG EWCEEDINEC
1310 1320 1330 1340 1350
ASDPCINGGL CRDLVNRFLC ICDVAFAGER CELDLADDRL LGIFTAVGSG
1360 1370 1380 1390 1400
TLALFFILLL AGVASLIASN KRATQGTYSP SGQEKAGPRV EMWIRMPPPA

LERLI
Length:1,405
Mass (Da):153,350
Last modified:July 27, 2011 - v3
Checksum:iFE1ECCB17529797B
GO
Isoform 2 (identifier: Q8VHS2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-389: Missing.
     1298-1376: NECASDPCIN...IASNKRATQG → EASVPPIPAS...VVEWGAQENY
     1377-1405: Missing.

Show »
Length:1,315
Mass (Da):144,240
Checksum:iA7BFB777507D5D50
GO
Isoform 3 (identifier: Q8VHS2-3) [UniParc]FASTAAdd to Basket

Also known as: Crb1s

The sequence of this isoform differs from the canonical sequence as follows:
     709-761: EYVAGRFGQD...LALENSTYQY → GERSGVPQSA...EIKWHSHDMY
     762-1405: Missing.

Show »
Length:761
Mass (Da):82,539
Checksum:i237635C3735E06A8
GO
Isoform 4 (identifier: Q8VHS2-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-372: Missing.
     373-389: SYVGASGYVCICQPGFT → MFGHKTQGFHILMAVLI
     709-761: EYVAGRFGQD...LALENSTYQY → GERSGVPQSA...EIKWHSHDMY
     762-1405: Missing.

Note: No experimental confirmation available.

Show »
Length:389
Mass (Da):42,611
Checksum:i79E07040792E01A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461K → E in AAL65131. (PubMed:11744384)Curated
Sequence conflicti46 – 461K → E in AAR20495. (PubMed:14684155)Curated
Sequence conflicti157 – 1571H → L in AAL65131. (PubMed:11744384)Curated
Sequence conflicti214 – 2141E → K in AAR20495. (PubMed:14684155)Curated
Sequence conflicti261 – 2611S → T in AAR20495. (PubMed:14684155)Curated
Sequence conflicti344 – 3441S → N in AAR20495. (PubMed:14684155)Curated
Sequence conflicti371 – 3711S → T in AAR20495. (PubMed:14684155)Curated
Sequence conflicti413 – 4131N → S in AAL65131. (PubMed:11744384)Curated
Sequence conflicti521 – 5211Missing in AAR20495. (PubMed:14684155)Curated
Sequence conflicti536 – 5361L → W in AAQ06606. 1 PublicationCurated
Sequence conflicti540 – 5401C → G in AAQ06606. 1 PublicationCurated
Sequence conflicti545 – 5451I → M in AAQ06606. 1 PublicationCurated
Sequence conflicti572 – 5721T → P in AAQ06606. 1 PublicationCurated
Sequence conflicti591 – 5911T → A in AAQ06606. 1 PublicationCurated
Sequence conflicti673 – 6731D → DD in AAR20495. (PubMed:14684155)Curated
Sequence conflicti741 – 7411F → L in AAQ06606. 1 PublicationCurated
Sequence conflicti745 – 7451R → H in AAQ06606. 1 PublicationCurated
Sequence conflicti835 – 8351P → L in AAQ06606. 1 PublicationCurated
Sequence conflicti886 – 8861G → R in AAQ06606. 1 PublicationCurated
Sequence conflicti900 – 9023VCH → ACR in AAQ06606. 1 PublicationCurated
Sequence conflicti942 – 9421P → S in AAQ06606. 1 PublicationCurated
Sequence conflicti982 – 9821H → Q in AAQ06606. 1 PublicationCurated
Sequence conflicti1062 – 10621I → V in AAQ06606. 1 PublicationCurated
Sequence conflicti1275 – 12751M → V in AAQ06606. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 372372Missing in isoform 4. 1 PublicationVSP_014730Add
BLAST
Alternative sequencei329 – 38961Missing in isoform 2. 1 PublicationVSP_014731Add
BLAST
Alternative sequencei373 – 38917SYVGA…QPGFT → MFGHKTQGFHILMAVLI in isoform 4. 1 PublicationVSP_014732Add
BLAST
Alternative sequencei709 – 76153EYVAG…STYQY → GERSGVPQSAVPLSRAISNH PGCRPLLGNIRTPQDLCWYL FTNEIKWHSHDMY in isoform 3 and isoform 4. 2 PublicationsVSP_014733Add
BLAST
Alternative sequencei762 – 1405644Missing in isoform 3 and isoform 4. 2 PublicationsVSP_014734Add
BLAST
Alternative sequencei1298 – 137679NECAS…RATQG → EASVPPIPASMEDCAGTWST GSYASVMWPSLGERCELDVS GLSFYVSLLLWQNLFQLLSY LVLHMNDEPVVEWGAQENY in isoform 2. 1 PublicationVSP_014735Add
BLAST
Alternative sequencei1377 – 140529Missing in isoform 2. 1 PublicationVSP_014736Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF406641 mRNA. Translation: AAL65131.1.
AY450552 mRNA. Translation: AAR20495.1.
AF492496 mRNA. Translation: AAQ06606.1.
AK044345 mRNA. Translation: BAC31879.1.
AK044704 mRNA. Translation: BAC32041.1.
AL606536, AC116810, AC138741 Genomic DNA. Translation: CAX16031.1.
CH466520 Genomic DNA. Translation: EDL39531.1.
CCDSiCCDS15336.1. [Q8VHS2-1]
RefSeqiNP_573502.2. NM_133239.2. [Q8VHS2-1]
UniGeneiMm.95700.

Genome annotation databases

EnsembliENSMUST00000059825; ENSMUSP00000060769; ENSMUSG00000063681. [Q8VHS2-1]
GeneIDi170788.
KEGGimmu:170788.
UCSCiuc007cwc.1. mouse. [Q8VHS2-1]
uc007cwe.1. mouse. [Q8VHS2-4]
uc007cwf.1. mouse. [Q8VHS2-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF406641 mRNA. Translation: AAL65131.1 .
AY450552 mRNA. Translation: AAR20495.1 .
AF492496 mRNA. Translation: AAQ06606.1 .
AK044345 mRNA. Translation: BAC31879.1 .
AK044704 mRNA. Translation: BAC32041.1 .
AL606536 , AC116810 , AC138741 Genomic DNA. Translation: CAX16031.1 .
CH466520 Genomic DNA. Translation: EDL39531.1 .
CCDSi CCDS15336.1. [Q8VHS2-1 ]
RefSeqi NP_573502.2. NM_133239.2. [Q8VHS2-1 ]
UniGenei Mm.95700.

3D structure databases

ProteinModelPortali Q8VHS2.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8VHS2.

Proteomic databases

PRIDEi Q8VHS2.

Protocols and materials databases

DNASUi 170788.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000059825 ; ENSMUSP00000060769 ; ENSMUSG00000063681 . [Q8VHS2-1 ]
GeneIDi 170788.
KEGGi mmu:170788.
UCSCi uc007cwc.1. mouse. [Q8VHS2-1 ]
uc007cwe.1. mouse. [Q8VHS2-4 ]
uc007cwf.1. mouse. [Q8VHS2-3 ]

Organism-specific databases

CTDi 23418.
MGIi MGI:2136343. Crb1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118786.
HOGENOMi HOG000230899.
HOVERGENi HBG080001.
InParanoidi Q8VHS2.
KOi K16681.
OMAi ATFLNDS.
OrthoDBi EOG7KH9HX.
TreeFami TF316224.

Miscellaneous databases

NextBioi 370423.
PROi Q8VHS2.
SOURCEi Search...

Gene expression databases

Bgeei Q8VHS2.
CleanExi MM_CRB1.
ExpressionAtlasi Q8VHS2. baseline.
Genevestigatori Q8VHS2.

Family and domain databases

Gene3Di 2.60.120.200. 3 hits.
InterProi IPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF00008. EGF. 11 hits.
PF12661. hEGF. 2 hits.
PF02210. Laminin_G_2. 3 hits.
[Graphical view ]
SMARTi SM00181. EGF. 10 hits.
SM00179. EGF_CA. 7 hits.
SM00282. LamG. 3 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 3 hits.
SSF57184. SSF57184. 1 hit.
PROSITEi PS00010. ASX_HYDROXYL. 10 hits.
PS00022. EGF_1. 15 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 17 hits.
PS01187. EGF_CA. 6 hits.
PS50025. LAM_G_DOMAIN. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of Crb1, a mouse homologue of Drosophila crumbs, and analysis of its expression pattern in eye and brain."
    den Hollander A.I., Ghiani M., de Kok Y.J.M., Wijnholds J., Ballabio A., Cremers F.P.M., Broccoli V.
    Mech. Dev. 110:203-207(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
    Tissue: Eye.
  2. "Expression of a novel secretory form (Crb1s) of mouse Crumbs homologue Crb1 in skin development."
    Watanabe T., Miyatani S., Katoh I., Kobayashi S., Ikawa Y.
    Biochem. Biophys. Res. Commun. 313:263-270(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
    Strain: ICR.
    Tissue: Skin.
  3. "Mouse Crumbs-2 in developing nervous system."
    Chang C.-H., Fan S.-S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: ICR.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Strain: C57BL/6J.
    Tissue: Retina.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Crumbs, the Drosophila homologue of human CRB1/RP12, is essential for photoreceptor morphogenesis."
    Pellikka M., Tanentzapf G., Pinto M., Smith C., McGlade C.J., Ready D.F., Tepass U.
    Nature 416:143-149(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "CRB1 is essential for external limiting membrane integrity and photoreceptor morphogenesis in the mammalian retina."
    Mehalow A.K., Kameya S., Smith R.S., Hawes N.L., Denegre J.M., Young J.A., Bechtold L., Haider N.B., Tepass U., Heckenlively J.R., Chang B., Naggert J.K., Nishina P.M.
    Hum. Mol. Genet. 12:2179-2189(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISEASE, FUNCTION.
  9. "Crumbs homologue 1 is required for maintenance of photoreceptor cell polarization and adhesion during light exposure."
    van de Pavert S.A., Kantardzhieva A., Malysheva A., Meuleman J., Versteeg I., Levelt C., Klooster J., Geiger S., Seeliger M.W., Rashbass P., Le Bivic A., Wijnholds J.
    J. Cell Sci. 117:4169-4177(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, COMPLEX FORMATION WITH MPDZ; MPP4 AND MPP5, FUNCTION.

Entry informationi

Entry nameiCRUM1_MOUSE
AccessioniPrimary (citable) accession number: Q8VHS2
Secondary accession number(s): B7ZC63
, Q6ST50, Q71JF2, Q8BGR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3