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Database: UniProt
Entry: Q8VHS2
LinkDB: Q8VHS2
Original site: Q8VHS2 
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   13-FEB-2019, entry version 151.
DE   RecName: Full=Protein crumbs homolog 1;
DE   Flags: Precursor;
GN   Name=Crb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
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.,
RA   Ballabio A., Cremers F.P.M., Broccoli V.;
RT   "Isolation of Crb1, a mouse homologue of Drosophila crumbs, and
RT   analysis of its expression pattern in eye and brain.";
RL   Mech. Dev. 110:203-207(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND FUNCTION.
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
RT   homologue 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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.,
RA   Ready D.F., 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   SUBCELLULAR LOCATION, DISEASE, AND FUNCTION.
RX   PubMed=12915475; DOI=10.1093/hmg/ddg232;
RA   Mehalow A.K., Kameya S., Smith R.S., Hawes N.L., Denegre J.M.,
RA   Young J.A., Bechtold L., Haider N.B., Tepass U., Heckenlively J.R.,
RA   Chang B., 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   SUBCELLULAR LOCATION, COMPLEX FORMATION WITH MPDZ; MPP4 AND MPP5, AND
RP   FUNCTION.
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.,
RA   Rashbass P., 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).
CC   -!- FUNCTION: Plays a role in photoreceptor morphogenesis in the
CC       retina. May maintain cell polarization and adhesion. Isoform 3
CC       could play a role in epidermal tissue morphogenesis. May function
CC       in cell attachment for stratified epithelial organization.
CC       {ECO:0000269|PubMed:12915475, ECO:0000269|PubMed:14684155,
CC       ECO:0000269|PubMed:15316081}.
CC   -!- SUBUNIT: In photoreceptor cells, forms a complex with MPDZ, MPP4
CC       and MPP5.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I
CC       membrane protein. Note=In the retina, localizes to the Mueller
CC       cell radial processes in the inner nuclear layer and in apical
CC       processes sclerad to the external limiting membrane. Localizes to
CC       the subapical region, adjacent to the adherens junction of
CC       photoreceptors. Isoform 3 which is secreted is found in the
CC       cytoplasmic area of undifferentiated keratinocytes and associates
CC       with the plasma membrane at the site of cell-cell contacts and
CC       focal adhesion upon keratinocytes differentiation.
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;
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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in brain and
CC       proliferative retinoblasts of the eye. In the brain, expressed in
CC       the granular layer of the cerebellum, the hippocampal dentate
CC       gyrus, the olfactory bulbs, the subventricular region lining the
CC       telencephalic ventricles and the rostral migratory stream. Isoform
CC       3 is ubiquitously expressed. {ECO:0000269|PubMed:11744384,
CC       ECO:0000269|PubMed:14684155}.
CC   -!- DEVELOPMENTAL STAGE: Primarily detected in the central nervous
CC       system at 10.5 dpc, in the ventral part of the neural tube
CC       including the ventral spinal cord, the ventral part of the
CC       mesencephalon, the mammillary and the hypothalamic regions, the
CC       optic area and the zona limitans intrathalamica. Expressed by the
CC       V3 interneurons placed between the floor plate and the
CC       motorneurons all along the spinal cord axis. In late
CC       embryogenesis, expressed mainly in ventral neural structures of
CC       the developing brain, including the mammillary, tuberalis regions
CC       of the hypothalamus and the preoptic area. Starting from 12.5 dpc,
CC       also strongly expressed in the neural area that gives rise to the
CC       dorsal thalamus. In the retina, expression starts at 11.5 dpc and
CC       is enhanced at 12.5, 14.5 and 16.5 dpc. In postnatal stages and in
CC       the adult eye, it is strongly expressed in photoreceptors and also
CC       found in inner nuclear layer and iris. Isoform 3 expression starts
CC       at 14 dpc, is enhanced at 15 and 16 dpc during active
CC       proliferation of epidermal cells, decreases after birth but is
CC       maintained in adult skin. Detected in the skin basal cells at 16
CC       dpc, it was observed in upper layers after birth (at protein
CC       level). {ECO:0000269|PubMed:11744384,
CC       ECO:0000269|PubMed:14684155}.
CC   -!- PTM: Glycosylated. {ECO:0000305}.
CC   -!- DISEASE: Note=Defects in Crb1 are a cause of focal retinal
CC       dysplasia and degeneration associated with a shortening of inner
CC       and outer segments. Affected mice produce a secreted truncated
CC       protein that lacks the single transmembrane and the intracellular
CC       domain, and develop irregularities at the outer limiting membrane
CC       and loss of photoreceptor cells. {ECO:0000269|PubMed:12915475}.
CC   -!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}.
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; AL606536; CAX16031.1; -; Genomic_DNA.
DR   EMBL; AC116810; CAX16031.1; JOINED; Genomic_DNA.
DR   EMBL; AC138741; CAX16031.1; JOINED; 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   UniGene; Mm.95700; -.
DR   ProteinModelPortal; Q8VHS2; -.
DR   SMR; Q8VHS2; -.
DR   CORUM; Q8VHS2; -.
DR   STRING; 10090.ENSMUSP00000060769; -.
DR   iPTMnet; Q8VHS2; -.
DR   PhosphoSitePlus; Q8VHS2; -.
DR   PaxDb; Q8VHS2; -.
DR   PRIDE; Q8VHS2; -.
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   eggNOG; ENOG410IR70; Eukaryota.
DR   eggNOG; ENOG411193Y; LUCA.
DR   GeneTree; ENSGT00940000155152; -.
DR   HOGENOM; HOG000230899; -.
DR   HOVERGEN; HBG080001; -.
DR   InParanoid; Q8VHS2; -.
DR   KO; K16681; -.
DR   OMA; SRVEMWS; -.
DR   OrthoDB; 111153at2759; -.
DR   TreeFam; TF316224; -.
DR   PRO; PR:Q8VHS2; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000063681; Expressed in 136 organ(s), highest expression level in retina.
DR   ExpressionAtlas; Q8VHS2; baseline and differential.
DR   Genevisible; Q8VHS2; MM.
DR   GO; GO:0005913; C:cell-cell adherens junction; ISO: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:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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: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:0007009; P:plasma membrane organization; IMP:MGI.
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; 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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28   1405       Protein crumbs homolog 1.
FT                                /FTId=PRO_0000007501.
FT   TOPO_DOM     28   1339       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1340   1360       Helical. {ECO:0000255}.
FT   TOPO_DOM   1361   1405       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       30     67       EGF-like 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN       69    107       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      109    145       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      147    183       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      185    221       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      223    259       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      261    298       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      300    336       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      338    394       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      396    438       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      440    480       EGF-like 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      482    669       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      671    707       EGF-like 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      713    884       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      886    922       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      923    959       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      950   1136       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1138   1174       EGF-like 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1176   1211       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1213   1249       EGF-like 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1254   1294       EGF-like 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1296   1332       EGF-like 19; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CARBOHYD     41     41       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    560    560       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    656    656       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    756    756       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    879    879       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    967    967       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    974    974       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    999    999       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1189   1189       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1242   1242       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1264   1264       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     34     45       {ECO:0000250}.
FT   DISULFID     39     54       {ECO:0000250}.
FT   DISULFID     55     66       {ECO:0000250}.
FT   DISULFID     73     84       {ECO:0000250}.
FT   DISULFID     78     95       {ECO:0000250}.
FT   DISULFID     97    106       {ECO:0000250}.
FT   DISULFID    113    124       {ECO:0000250}.
FT   DISULFID    118    133       {ECO:0000250}.
FT   DISULFID    135    144       {ECO:0000250}.
FT   DISULFID    151    162       {ECO:0000250}.
FT   DISULFID    156    171       {ECO:0000250}.
FT   DISULFID    173    182       {ECO:0000250}.
FT   DISULFID    189    200       {ECO:0000250}.
FT   DISULFID    194    209       {ECO:0000250}.
FT   DISULFID    211    220       {ECO:0000250}.
FT   DISULFID    227    238       {ECO:0000250}.
FT   DISULFID    232    247       {ECO:0000250}.
FT   DISULFID    249    258       {ECO:0000250}.
FT   DISULFID    265    276       {ECO:0000250}.
FT   DISULFID    270    285       {ECO:0000250}.
FT   DISULFID    287    297       {ECO:0000250}.
FT   DISULFID    304    315       {ECO:0000250}.
FT   DISULFID    309    324       {ECO:0000250}.
FT   DISULFID    326    335       {ECO:0000250}.
FT   DISULFID    342    353       {ECO:0000250}.
FT   DISULFID    347    382       {ECO:0000250}.
FT   DISULFID    384    393       {ECO:0000250}.
FT   DISULFID    400    411       {ECO:0000250}.
FT   DISULFID    405    420       {ECO:0000250}.
FT   DISULFID    422    437       {ECO:0000250}.
FT   DISULFID    444    455       {ECO:0000250}.
FT   DISULFID    449    468       {ECO:0000250}.
FT   DISULFID    470    479       {ECO:0000250}.
FT   DISULFID    641    669       {ECO:0000250}.
FT   DISULFID    675    686       {ECO:0000250}.
FT   DISULFID    680    695       {ECO:0000250}.
FT   DISULFID    697    706       {ECO:0000250}.
FT   DISULFID    850    884       {ECO:0000250}.
FT   DISULFID    890    901       {ECO:0000250}.
FT   DISULFID    895    910       {ECO:0000250}.
FT   DISULFID    912    921       {ECO:0000250}.
FT   DISULFID    927    938       {ECO:0000250}.
FT   DISULFID    932    947       {ECO:0000250}.
FT   DISULFID   1095   1136       {ECO:0000250}.
FT   DISULFID   1142   1153       {ECO:0000250}.
FT   DISULFID   1147   1162       {ECO:0000250}.
FT   DISULFID   1164   1173       {ECO:0000250}.
FT   DISULFID   1180   1190       {ECO:0000250}.
FT   DISULFID   1185   1199       {ECO:0000250}.
FT   DISULFID   1201   1210       {ECO:0000250}.
FT   DISULFID   1217   1228       {ECO:0000250}.
FT   DISULFID   1222   1237       {ECO:0000250}.
FT   DISULFID   1239   1248       {ECO:0000250}.
FT   DISULFID   1258   1273       {ECO:0000250}.
FT   DISULFID   1267   1282       {ECO:0000250}.
FT   DISULFID   1284   1293       {ECO:0000250}.
FT   DISULFID   1300   1311       {ECO:0000250}.
FT   DISULFID   1305   1320       {ECO:0000250}.
FT   DISULFID   1322   1331       {ECO:0000250}.
FT   VAR_SEQ       1    372       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_014730.
FT   VAR_SEQ     329    389       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_014731.
FT   VAR_SEQ     373    389       SYVGASGYVCICQPGFT -> MFGHKTQGFHILMAVLI
FT                                (in isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_014732.
FT   VAR_SEQ     709    761       EYVAGRFGQDDSTGYAAFSVNDNYGQNFSLSMFVRTRQPLG
FT                                LLLALENSTYQY -> GERSGVPQSAVPLSRAISNHPGCRP
FT                                LLGNIRTPQDLCWYLFTNEIKWHSHDMY (in isoform
FT                                3 and isoform 4).
FT                                {ECO:0000303|PubMed:14684155,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_014733.
FT   VAR_SEQ     762   1405       Missing (in isoform 3 and isoform 4).
FT                                {ECO:0000303|PubMed:14684155,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_014734.
FT   VAR_SEQ    1298   1376       NECASDPCINGGLCRDLVNRFLCICDVAFAGERCELDLADD
FT                                RLLGIFTAVGSGTLALFFILLLAGVASLIASNKRATQG ->
FT                                EASVPPIPASMEDCAGTWSTGSYASVMWPSLGERCELDVSG
FT                                LSFYVSLLLWQNLFQLLSYLVLHMNDEPVVEWGAQENY
FT                                (in isoform 2). {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_014735.
FT   VAR_SEQ    1377   1405       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_014736.
FT   CONFLICT     46     46       K -> E (in Ref. 1; AAL65131 and 2;
FT                                AAR20495). {ECO:0000305}.
FT   CONFLICT    157    157       H -> L (in Ref. 1; AAL65131).
FT                                {ECO:0000305}.
FT   CONFLICT    214    214       E -> K (in Ref. 2; AAR20495).
FT                                {ECO:0000305}.
FT   CONFLICT    261    261       S -> T (in Ref. 2; AAR20495).
FT                                {ECO:0000305}.
FT   CONFLICT    344    344       S -> N (in Ref. 2; AAR20495).
FT                                {ECO:0000305}.
FT   CONFLICT    371    371       S -> T (in Ref. 2; AAR20495).
FT                                {ECO:0000305}.
FT   CONFLICT    413    413       N -> S (in Ref. 1; AAL65131).
FT                                {ECO:0000305}.
FT   CONFLICT    521    521       Missing (in Ref. 2; AAR20495).
FT                                {ECO:0000305}.
FT   CONFLICT    536    536       L -> W (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    540    540       C -> G (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    545    545       I -> M (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    572    572       T -> P (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    591    591       T -> A (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    673    673       D -> DD (in Ref. 2; AAR20495).
FT                                {ECO:0000305}.
FT   CONFLICT    741    741       F -> L (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    745    745       R -> H (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    835    835       P -> L (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    886    886       G -> R (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    900    902       VCH -> ACR (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    942    942       P -> S (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT    982    982       H -> Q (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT   1062   1062       I -> V (in Ref. 3; AAQ06606).
FT                                {ECO:0000305}.
FT   CONFLICT   1275   1275       M -> V (in Ref. 3; AAQ06606).
FT                                {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
//
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