Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8VHS2 (CRUM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein crumbs homolog 1
Gene names
Name:Crb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1405 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.8 Ref.9

Subunit structure

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

Subcellular location

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. Ref.1 Ref.7 Ref.8 Ref.9

Tissue specificity

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. Ref.1 Ref.2

Developmental stage

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). Ref.1 Ref.2

Post-translational modification

Glycosylated Probable.

Involvement in disease

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. Ref.8

Sequence similarities

Belongs to the Crumbs protein family.

Contains 19 EGF-like domains.

Contains 3 laminin G-like domains.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VHS2-1)

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.
Isoform 2 (identifier: Q8VHS2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     329-389: Missing.
     1298-1376: NECASDPCIN...IASNKRATQG → EASVPPIPAS...VVEWGAQENY
     1377-1405: Missing.
Isoform 3 (identifier: Q8VHS2-3)

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.
Isoform 4 (identifier: Q8VHS2-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 14051378Protein crumbs homolog 1
PRO_0000007501

Regions

Topological domain28 – 13391312Extracellular Potential
Transmembrane1340 – 136021Helical; Potential
Topological domain1361 – 140545Cytoplasmic Potential
Domain30 – 6738EGF-like 1; atypical
Domain69 – 10739EGF-like 2
Domain109 – 14537EGF-like 3
Domain147 – 18337EGF-like 4; calcium-binding Potential
Domain185 – 22137EGF-like 5; calcium-binding Potential
Domain223 – 25937EGF-like 6; calcium-binding Potential
Domain261 – 29838EGF-like 7
Domain300 – 33637EGF-like 8
Domain338 – 39457EGF-like 9
Domain396 – 43843EGF-like 10
Domain440 – 48041EGF-like 11
Domain482 – 669188Laminin G-like 1
Domain671 – 70737EGF-like 12
Domain713 – 884172Laminin G-like 2
Domain886 – 92237EGF-like 13
Domain923 – 95937EGF-like 14
Domain950 – 1136187Laminin G-like 3
Domain1138 – 117437EGF-like 15
Domain1176 – 121136EGF-like 16; calcium-binding Potential
Domain1213 – 124937EGF-like 17
Domain1254 – 129441EGF-like 18
Domain1296 – 133237EGF-like 19; calcium-binding Potential

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation5601N-linked (GlcNAc...) Potential
Glycosylation6561N-linked (GlcNAc...) Potential
Glycosylation7561N-linked (GlcNAc...) Potential
Glycosylation8791N-linked (GlcNAc...) Potential
Glycosylation9671N-linked (GlcNAc...) Potential
Glycosylation9741N-linked (GlcNAc...) Potential
Glycosylation9991N-linked (GlcNAc...) Potential
Glycosylation11891N-linked (GlcNAc...) Potential
Glycosylation12421N-linked (GlcNAc...) Potential
Glycosylation12641N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 45 By similarity
Disulfide bond39 ↔ 54 By similarity
Disulfide bond55 ↔ 66 By similarity
Disulfide bond73 ↔ 84 By similarity
Disulfide bond78 ↔ 95 By similarity
Disulfide bond97 ↔ 106 By similarity
Disulfide bond113 ↔ 124 By similarity
Disulfide bond118 ↔ 133 By similarity
Disulfide bond135 ↔ 144 By similarity
Disulfide bond151 ↔ 162 By similarity
Disulfide bond156 ↔ 171 By similarity
Disulfide bond173 ↔ 182 By similarity
Disulfide bond189 ↔ 200 By similarity
Disulfide bond194 ↔ 209 By similarity
Disulfide bond211 ↔ 220 By similarity
Disulfide bond227 ↔ 238 By similarity
Disulfide bond232 ↔ 247 By similarity
Disulfide bond249 ↔ 258 By similarity
Disulfide bond265 ↔ 276 By similarity
Disulfide bond270 ↔ 285 By similarity
Disulfide bond287 ↔ 297 By similarity
Disulfide bond304 ↔ 315 By similarity
Disulfide bond309 ↔ 324 By similarity
Disulfide bond326 ↔ 335 By similarity
Disulfide bond342 ↔ 353 By similarity
Disulfide bond347 ↔ 382 By similarity
Disulfide bond384 ↔ 393 By similarity
Disulfide bond400 ↔ 411 By similarity
Disulfide bond405 ↔ 420 By similarity
Disulfide bond422 ↔ 437 By similarity
Disulfide bond444 ↔ 455 By similarity
Disulfide bond449 ↔ 468 By similarity
Disulfide bond470 ↔ 479 By similarity
Disulfide bond641 ↔ 669 By similarity
Disulfide bond675 ↔ 686 By similarity
Disulfide bond680 ↔ 695 By similarity
Disulfide bond697 ↔ 706 By similarity
Disulfide bond850 ↔ 884 By similarity
Disulfide bond890 ↔ 901 By similarity
Disulfide bond895 ↔ 910 By similarity
Disulfide bond912 ↔ 921 By similarity
Disulfide bond927 ↔ 938 By similarity
Disulfide bond932 ↔ 947 By similarity
Disulfide bond1095 ↔ 1136 By similarity
Disulfide bond1142 ↔ 1153 By similarity
Disulfide bond1147 ↔ 1162 By similarity
Disulfide bond1164 ↔ 1173 By similarity
Disulfide bond1180 ↔ 1190 By similarity
Disulfide bond1185 ↔ 1199 By similarity
Disulfide bond1201 ↔ 1210 By similarity
Disulfide bond1217 ↔ 1228 By similarity
Disulfide bond1222 ↔ 1237 By similarity
Disulfide bond1239 ↔ 1248 By similarity
Disulfide bond1258 ↔ 1273 By similarity
Disulfide bond1267 ↔ 1282 By similarity
Disulfide bond1284 ↔ 1293 By similarity
Disulfide bond1300 ↔ 1311 By similarity
Disulfide bond1305 ↔ 1320 By similarity
Disulfide bond1322 ↔ 1331 By similarity

Natural variations

Alternative sequence1 – 372372Missing in isoform 4.
VSP_014730
Alternative sequence329 – 38961Missing in isoform 2.
VSP_014731
Alternative sequence373 – 38917SYVGA…QPGFT → MFGHKTQGFHILMAVLI in isoform 4.
VSP_014732
Alternative sequence709 – 76153EYVAG…STYQY → GERSGVPQSAVPLSRAISNH PGCRPLLGNIRTPQDLCWYL FTNEIKWHSHDMY in isoform 3 and isoform 4.
VSP_014733
Alternative sequence762 – 1405644Missing in isoform 3 and isoform 4.
VSP_014734
Alternative sequence1298 – 137679NECAS…RATQG → EASVPPIPASMEDCAGTWST GSYASVMWPSLGERCELDVS GLSFYVSLLLWQNLFQLLSY LVLHMNDEPVVEWGAQENY in isoform 2.
VSP_014735
Alternative sequence1377 – 140529Missing in isoform 2.
VSP_014736

Experimental info

Sequence conflict461K → E in AAL65131. Ref.1
Sequence conflict461K → E in AAR20495. Ref.2
Sequence conflict1571H → L in AAL65131. Ref.1
Sequence conflict2141E → K in AAR20495. Ref.2
Sequence conflict2611S → T in AAR20495. Ref.2
Sequence conflict3441S → N in AAR20495. Ref.2
Sequence conflict3711S → T in AAR20495. Ref.2
Sequence conflict4131N → S in AAL65131. Ref.1
Sequence conflict5211Missing in AAR20495. Ref.2
Sequence conflict5361L → W in AAQ06606. Ref.3
Sequence conflict5401C → G in AAQ06606. Ref.3
Sequence conflict5451I → M in AAQ06606. Ref.3
Sequence conflict5721T → P in AAQ06606. Ref.3
Sequence conflict5911T → A in AAQ06606. Ref.3
Sequence conflict6731D → DD in AAR20495. Ref.2
Sequence conflict7411F → L in AAQ06606. Ref.3
Sequence conflict7451R → H in AAQ06606. Ref.3
Sequence conflict8351P → L in AAQ06606. Ref.3
Sequence conflict8861G → R in AAQ06606. Ref.3
Sequence conflict900 – 9023VCH → ACR in AAQ06606. Ref.3
Sequence conflict9421P → S in AAQ06606. Ref.3
Sequence conflict9821H → Q in AAQ06606. Ref.3
Sequence conflict10621I → V in AAQ06606. Ref.3
Sequence conflict12751M → V in AAQ06606. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: FE1ECCB17529797B

FASTA1,405153,350
        10         20         30         40         50         60 
MKLKRTAYLL FLYLSSSLLI CIKNSFCNKN NTRCLSGPCQ NNSTCKHFPQ DNNCCLDTAN 

        70         80         90        100        110        120 
NLDKDCEDLK DPCFSSPCQG IATCVKIPGE GNFLCQCPPG YSGLNCETAT NSCGGNLCQH 

       130        140        150        160        170        180 
GGTCRKDPEH PVCICPPGYA GRFCETDHNE CASSPCHNGA MCQDGINGYS CFCVPGYQGR 

       190        200        210        220        230        240 
HCDLEVDECV SDPCKNEAVC LNEIGRYTCV CPQEFSGVNC ELEIDECRSQ PCLHGATCQD 

       250        260        270        280        290        300 
APGGYSCDCA PGFLGEHCEL SVNECESQPC LHGGLCVDGR NSYHCDCTGS GFTGMHCESL 

       310        320        330        340        350        360 
IPLCWSKPCH NDATCEDTVD SYICHCRPGY TGALCETDIN ECSSNPCQFW GECVELSSEG 

       370        380        390        400        410        420 
LYGNTAGLPS SFSYVGASGY VCICQPGFTG IHCEEDVDEC LLHPCLNGGT CENLPGNYAC 

       430        440        450        460        470        480 
HCPFDDTSRT FYGGENCSEI LLGCTHHQCL NNGKCIPHFQ NGQHGFTCQC LSGYAGPLCE 

       490        500        510        520        530        540 
TVTTLSFGSN GFLWVTSGSH TGIGPECNIS LRFHTVQPNA LLLIRGNKDV SMKLELLNGC 

       550        560        570        580        590        600 
VHLSIEVWNQ LKVLLSISHN TSDGEWHFVE VTIAETLTLA LVGGSCKEKC TTKSSVPVEN 

       610        620        630        640        650        660 
HQSICALQDS FLGGLPMGTA NNSVSVLNIY NVPSTPSFVG CLQDIRFDLN HITLENVSSG 

       670        680        690        700        710        720 
LSSNVKAGCL GKDWCESQPC QNRGRCINLW QGYQCECDRP YTGSNCLKEY VAGRFGQDDS 

       730        740        750        760        770        780 
TGYAAFSVND NYGQNFSLSM FVRTRQPLGL LLALENSTYQ YVSVWLEHGS LALQTPGSPK 

       790        800        810        820        830        840 
FMVNFFLSDG NVHLISLRIK PNEIELYQSS QNLGFISVPT WTIRRGDVIF IGGLPDREKT 

       850        860        870        880        890        900 
EVYGGFFKGC VQDVRLNSQT LEFFPNSTNN AYDDPILVNV TQGCPGDNTC KSNPCHNGGV 

       910        920        930        940        950        960 
CHSLWDDFSC SCPTNTAGRA CEQVQWCQLS PCPPTAECQL LPQGFECIAN AVFSGLSREI 

       970        980        990       1000       1010       1020 
LFRSNGNITR ELTNITFAFR THDTNVMILH AEKEPEFLNI SIQDARLFFQ LRSGNSFYTL 

      1030       1040       1050       1060       1070       1080 
HLMGSQLVND GTWHQVTFSM IDPVAQTSRW QMEVNDQTPF VISEVATGSL NFLKDNTDIY 

      1090       1100       1110       1120       1130       1140 
VGDQSVDNPK GLQGCLSTIE IGGIYLSYFE NLHGFPGKPQ EEQFLKVSTN MVLTGCLPSN 

      1150       1160       1170       1180       1190       1200 
ACHSSPCLHG GNCEDSYSSY RCACLSGWSG THCEINIDEC FSSPCIHGNC SDGVAAYHCR 

      1210       1220       1230       1240       1250       1260 
CEPGYTGVNC EVDVDNCKSH QCANGATCVP EAHGYSCLCF GNFTGRFCRH SRLPSTVCGN 

      1270       1280       1290       1300       1310       1320 
EKRNFTCYNG GSCSMFQEDW QCMCWPGFTG EWCEEDINEC ASDPCINGGL CRDLVNRFLC 

      1330       1340       1350       1360       1370       1380 
ICDVAFAGER CELDLADDRL LGIFTAVGSG TLALFFILLL AGVASLIASN KRATQGTYSP 

      1390       1400 
SGQEKAGPRV EMWIRMPPPA LERLI 

« Hide

Isoform 2 [UniParc].

Checksum: A7BFB777507D5D50
Show »

FASTA1,315144,240
Isoform 3 (Crb1s) [UniParc].

Checksum: 237635C3735E06A8
Show »

FASTA76182,539
Isoform 4 [UniParc].

Checksum: 79E07040792E01A8
Show »

FASTA38942,611

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_573502.2. NM_133239.2.
UniGeneMm.95700.

3D structure databases

ProteinModelPortalQ8VHS2.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8VHS2.

Proteomic databases

PRIDEQ8VHS2.

Protocols and materials databases

DNASU170788.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059825; ENSMUSP00000060769; ENSMUSG00000063681. [Q8VHS2-1]
GeneID170788.
KEGGmmu:170788.
UCSCuc007cwc.1. mouse. [Q8VHS2-1]
uc007cwe.1. mouse. [Q8VHS2-4]
uc007cwf.1. mouse. [Q8VHS2-3]

Organism-specific databases

CTD23418.
MGIMGI:2136343. Crb1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00750000117426.
HOGENOMHOG000230899.
HOVERGENHBG080001.
InParanoidQ8VHS2.
KOK16681.
OMAATFLNDS.
OrthoDBEOG7KH9HX.
TreeFamTF316224.

Gene expression databases

BgeeQ8VHS2.
CleanExMM_CRB1.
GenevestigatorQ8VHS2.

Family and domain databases

Gene3D2.60.120.200. 3 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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]
PfamPF00008. EGF. 11 hits.
PF12661. hEGF. 2 hits.
PF02210. Laminin_G_2. 3 hits.
[Graphical view]
SMARTSM00181. EGF. 10 hits.
SM00179. EGF_CA. 7 hits.
SM00282. LamG. 3 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 3 hits.
SSF57184. SSF57184. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

NextBio370423.
PROQ8VHS2.
SOURCESearch...

Entry information

Entry nameCRUM1_MOUSE
AccessionPrimary (citable) accession number: Q8VHS2
Secondary accession number(s): B7ZC63 expand/collapse secondary AC list , Q6ST50, Q71JF2, Q8BGR4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot