ID A0A3B4A9P1_9GOBI Unreviewed; 2551 AA.
AC A0A3B4A9P1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPMGP00000013226.1};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000013226.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000013226.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 409849.ENSPMGP00000013226; -.
DR Ensembl; ENSPMGT00000014116.1; ENSPMGP00000013226.1; ENSPMGG00000010895.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 14.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.60; Cadherins; 14.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF445; CADHERIN-87A; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 11.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 15.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 15.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 7.
DR PROSITE; PS50268; CADHERIN_2; 13.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003318};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2372..2393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..294
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 304..396
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 397..503
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 507..612
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 613..712
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 713..824
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 825..939
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 940..1041
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1042..1148
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1158..1268
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1269..1376
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1386..1482
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1482..1603
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1845..1884
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1885..2086
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2089..2128
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2131..2303
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2326..2362
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 2480..2529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2484..2513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1874..1883
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2118..2127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2330..2340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2352..2361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2551 AA; 281711 MW; 76A53A2D90665391 CRC64;
MNYSSLPVEN EIIFRQVALL GCTVDCPLKC VCIGSSSCVH SSKLTVPGLA RMGGWEHTGT
LACRGWLCPF HLKLYITHFS SHHFSIGPEW YLVRVELTVT DVNDNVPEWR MVPSPYLAVV
SSDAVGGTLV YKLYAEDGDE GNNGEVEYFL SDGGDGRFEV DRKSGHVRTT GLPLQRDREY
LLTVVAADRL GSRSAPVVVS VVAGERPPQF TNTSYTIAIP ENTPEGQTLL INPSSLFSIA
AETGEISLTR PIDYESDQHR YLLLVRASEE HDSMRSAAEV RVVIVDENDC VPEFLQSIYS
KDGVPETVTT ATSLLQVSAT DCDSEANAEL TYYTLSPDFS ISPHGTIFPA GPLDYERLNH
LYEFVVMAID KGDVPRTGTT TVRIRMANVN DEAPEFSQHI YRTFVSEDAG PNTLVATVLA
KDPDGDGITY KITSGNEEGN FVIDSQKGLI RLRSSPPPRL QGVEYVLNVT ATDDNASGGP
QALSTTAQVI VGVDDVNNNK PVFEKCQQYR ESTAVLENQP AGTFVLQVHA VDADEGSNGK
VTYGFMHKDS TVPAFSIHPD TGVIVTARKF DRERQREYAV TVTATDQAAD PLIGICQLNI
LILDQNDNSP KFENIRYEYF LREDTMIGNS FLRVAAHDDD FGTNAAVTYS MSNEQPEYLR
VNPLTGWVYV NQPISQRTYI TREIVATDGG NRTSSVELAV TITNVKNQPP QWEKDSYSVV
IPENTVRDTP VVTIKATSPL GDPRVTYNLE DGMVPETNMP VRFYLTPNRE DGSASILVAE
PLDYETTRNF MLRVRAQNVA AVPLAAFTTV YVNVTDVNDN VPFFTSSIYE ASVTEGAEAG
TMVFQVSAND LDLGQNGKIS YSLLEDRSGD YQYFRIDPEL GYIHTKTVFD RETKSSYLLE
VQSVDGYESA RPGKHGQPNS DTAYVRIFIS DVNDNKPAFA QASYEVDVDE DADVGFAVLT
VSANDGDEGG NAKLRYQITS GNTGGVFDVE PEVGTIFIAQ PLDYEQNKRY KLHLLASDGK
WEDYTSVAVN VVNKNDEAPV FTVNEYYGSV TEELDGSPVF VLQVTASDPD KDADQEALRY
SLHGQGADSE FIIDEVTGKI YAQRTLNRED RAVWRFVVLA TDESGEGLTG FTDVIINVWD
INDNAPIFTC APSCHGDVAE NSPPGTLVME MTATDLDDAA VGQNAVLSYR IVGSLDATNM
EVGGLPTFSD MFSINPTTGT ITVAMNGLDR EQVESYLLVV EARDGGGMTG TGTASIQIKD
VNDHAPRFTD HTCMAKVSEN AEPNSEVLEL AAEDRDTGEN AQLTFSVVAG DQEQKFYMIS
HKQEKRGTLR IKKRLDYERH NEQRFNLTLK VEDLDFSSLL HCVVEVEDYN DHSPVFIPHF
LSLAPLPEDI SVGTSVARMV ASDSDSGLNR DITYSLLEES DPDGLFTIDQ SGLLSVAQPL
DREKTAQHQL VVIATDHGTP SLTGSATVQL PLLDVNDNGP EFEAVYSPVV FENVAGPQVV
RLNQTSTLIR AVDQDSLENG PPFHFTVPAE YRHSNDFYLQ DNLNGTATLT ALRTFDRERQ
KEFLIPIIMS DSGRPAKTVT STLTVTIGDQ NDHAHVAGEK KIFINSHRGR MPTTVLGKVY
SPDPDDWDNK TYVFEGHVPN YFILNKRTGF LIIKENAPPG TYQFQVRVSD GVWPDAVSTV
TVHVRELRDE AIHSSGSLRL ADITAKEFID LRGKQRSRYD LLVDFLSEML SVPPDDVNIF
SLMDVRDRML DVRFAVHGPP LFLQPEKMHG YLAAHKQKLQ SFMQTSVSQV RVDECPSSEC
PGAGGCTTVL NVRDTPTVVD CGTMSLVSVT VESTAVCSCP GREQSHQPCA AYPRNPCYNG
GICVDTQHGY RCQCPAQFEG PECQQNKHSF HGNGYAWFPP MMPCFESHVS LEFITDVADG
LLLYSGPLAQ LQAWDYEDFM AIELIDGTPT LKINHGSGTV VLQLPGNVNV ADRRWHRLDV
RSNSKEVRFT LDRCAGAAVR EMEGVGSWLT TEDHSSCEVI GTTPNTDRHL NMSQVLQLGG
VNEDIPYIYP QLQHKHFTGC MRNLIVDSKL YDLGSPADSQ SSSPGCITTD SSCVNMGYPS
CGHRGRCHGE WGSFSCQCIP GYTGHQCEEV APEYSFDGNS HVHYQLTSLL PPRRTFVQVL
VRTRKHSSTI LSLISKEQNE YIRLEIFQGL LCVLYNLGDG EYNLTLPVYR LDNGEWHEVF
LDRHDNEMTL RLDGGGGQRE ITGSRGRSRE IIIDPSVIML GNTVPSGVNK SFQGSQPRDG
VSQFSVQGLS LGCSSDSCKR NQCSPPFTCV DLWRVHECRY GWKSCVYTLC ATRPCHRGTC
VAQSPSKFTC HCPEGYRGRH CETTLAIYRE DVGLSFSSLF AICICFMALL GMYRTILSYK
GLKEGVYHVS AHHDGWEDIR ENVLNYDEEG GGEEDQNAYD MAELQKSLQP SPAQSIQYCR
SRDLARYLCE IIRDADQHPD TGPFDSLQVF STEGGGSPAG SLSSFSSAGL DGTSSAEGAG
ETRREETLAD WGPRFEKLRA LYERGHLDGT Y
//