ID A0A2K6TQE7_SAIBB Unreviewed; 1405 AA.
AC A0A2K6TQE7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Crumbs cell polarity complex component 1 {ECO:0000313|Ensembl:ENSSBOP00000021802.1};
GN Name=CRB1 {ECO:0000313|Ensembl:ENSSBOP00000021802.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000021802.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000021802.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_003944187.1; XM_003944138.2.
DR STRING; 39432.ENSSBOP00000021802; -.
DR Ensembl; ENSSBOT00000038645.1; ENSSBOP00000021802.1; ENSSBOG00000027430.1.
DR GeneID; 101029876; -.
DR KEGG; sbq:101029876; -.
DR CTD; 23418; -.
DR GeneTree; ENSGT00940000155152; -.
DR OMA; NCTEFQG; -.
DR OrthoDB; 2877476at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0035003; C:subapical complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0071482; P:cellular response to light stimulus; IEA:Ensembl.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0061159; P:establishment of bipolar cell polarity involved in cell morphogenesis; IEA:Ensembl.
DR GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0010001; P:glial cell differentiation; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR GO; GO:0007009; P:plasma membrane organization; IEA:Ensembl.
DR GO; GO:0060060; P:post-embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 15.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.10.25.10; Laminin; 17.
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 PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR Pfam; PF00008; EGF; 13.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF02210; Laminin_G_2; 3.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 18.
DR SMART; SM00179; EGF_CA; 16.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 8.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
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; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1405
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014450370"
FT TRANSMEM 1343..1367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..108
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 110..146
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 148..184
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 186..222
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 224..260
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 262..299
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 301..337
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 339..394
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 396..438
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 440..480
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 484..669
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 671..707
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 713..884
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 886..922
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 949..1136
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1138..1174
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1176..1211
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1213..1249
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1254..1294
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1296..1332
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 79..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 98..107
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 136..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 174..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 212..221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 250..259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 327..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 384..393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 470..479
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 697..706
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 912..921
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1164..1173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1180..1190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1201..1210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1239..1248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1284..1293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1322..1331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1405 AA; 154012 MW; 863690C022A0B531 CRC64;
MALKNIKYFL IFYLSFSLLI YIKNSFCNRN TTRCLSNSCQ NNSTCNGFSK DNNCSCSDTT
SNLDKDCDNM KDPCFSNPCQ GSATCVNIPG ERSFLCKCPP GYSGTSCETT IGSCGMNSCQ
HGGICHQDPI YPVCICPAGY AGRFCEIDHD ECSSSPCQNG AMCQDGIDGY SCFCVPGYQG
RHCDLEVDEC ASDPCKNEAT CLNEIGRYTC ICPHDYSGVN CELEIDECWS QPCLNGANCR
DALGAYFCDC APGFLGDHCE LNIDECASQP CLHGGLCVDG ENRYSCNCTG SGFTGTHCET
VMPPCWSKPC HNNATCEDSV DNYTCHCWPG YTGVQCEIDI NECSSNPCQS DGECVELSSE
KRYGHIVGPP SFSYREASGY VCVCQPGFTG IHCEEDVNEC SSNPCQNSGT CENLPGNYTC
HCPFDNLSRT FYGGRDCSDI LLGCTHQQCL NNGICIPHFQ DGQHGFSCLC PSGYTGSLCE
TATTLSFEGD GFLWVTIDSV TTKDSVCSIA LRFQTVQPMA LLLFRGNREV FVKLELLSGY
IHLSIQVNNQ PKVLLYLSHN TSDGEWHFVE VIFAEAVTLT LIDDSCKEKC ITKAPSPFES
DQSICAFQNS FLGGLPVGRT SSGAALLNFY NIPSTPSFVG CLQDIKIDWN HITPENISSG
SSLNVKPGCV RKDWCESQPC QSRGHCINLW LSYQCDCHRP YKGSNCLREY VAGKFGQDDS
TGYAAFTLDE SHGDTVSLSM FVRTLHPSGL LLALGNSTYQ HIRVWLEHGR LGMLTPSSPK
LVVRFVLNDG NVHLITLKIK PNKIELYRSS QNLGFISAST WKIQKGDVIY IGGLPDRQET
ELNGGFFKGC IQDVRLNNQN LEFFSNSTNE ALHNPVLVNV TEGCPGDNFC KSNPCHNGGV
CHSLWDDFSC SCPANTSGKA CEEAQWCGLS PCPPRAQCQL VPQGFECIAN AVFHGQSSQI
LFRSNGNITR ELTNITFGFR TRNANVIILH AEKEPEFLNI SIQDSRLFFQ LQSGNSFHTL
SLTSLRSVND GMWHRVTLSM TDPLAQTSRW QMEVDNQTPF VTSTIATGSL NFLKDNTDIY
VGDRAIDNIK GLHGCLSTIE IGGIYLSYFE NVRGFTKKPQ EEQFLKISTP SVVTGCLQLN
ACNSNPCLHG GNCEDIYSSY HCSCPLGWSG KHCELNVDEC FSNPCIHGNC SDSVAAYHCR
CEPGYAGANC EVAIDHCRSH QCANGATCIS DTNGYSCLCL GNFTGKFCRQ RRLPSTVCGN
ERTNLTCYNG GNCTEFQAEL KCMCWPGFTG ERCEKDIDEC ASDPCVNGGL CQDLLNKFQC
LCDVAFAGER CEVDLADGLI SDVFTALGSV TLALLLILLL AVVASVVTSN KRATQGTYSP
NRQEKEGSRV EMWNLMPPPA MERLI
//
