ID H3ATN8_LATCH Unreviewed; 2519 AA.
AC H3ATN8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000013009.1};
GN Name=SI:CH211-186J3.6 {ECO:0000313|Ensembl:ENSLACP00000013009.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000013009.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000013009.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AFYH01092464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01092465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01092466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01092467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01092468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01092469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01092470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000013009; -.
DR Ensembl; ENSLACT00000013104.1; ENSLACP00000013009.1; ENSLACG00000011462.1.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000164020; -.
DR HOGENOM; CLU_000347_1_0_1; -.
DR InParanoid; H3ATN8; -.
DR OMA; EPWCAKV; -.
DR TreeFam; TF351842; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 15.
DR CDD; cd00054; EGF_CA; 4.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF422; NEURAL-CADHERIN 2-RELATED; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 13.
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; 4.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 15.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 7.
DR PROSITE; PS50268; CADHERIN_2; 14.
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 Reference proteome {ECO:0000313|Proteomes:UP000008672};
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 2328..2348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..124
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 125..225
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 235..327
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 328..434
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 444..543
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 544..642
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 644..755
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 756..870
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 871..972
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 973..1079
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1090..1192
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1193..1300
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1310..1406
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1406..1520
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1768..1807
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1808..2012
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2015..2054
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2057..2232
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2275..2311
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 2406..2426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1797..1806
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2044..2053
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2279..2289
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2301..2310
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2519 AA; 279937 MW; 259D4AFFFD444A55 CRC64;
GKDWYLMRIE LIVTDVNDNA PEWTMSPFPF LAVVSPDATA GTTVYTLLAQ DGDEGISGEV
EYFLLEGGDD RFEVDKKTGV IRTTGLPLEK DKEYLLTVLV ADKFSNEGPP AVVSVIAGPR
APQFFNLSYT VLIPENIPEG QPFLTVSALS FQNKSLSYSL IINPSNLFNV HQETGEINMI
QSVDYERDQH QYLMLVGVTE SQDQLSSAAE VLVVIIDVND CVPEFMQSIY SKDNVPETVT
TATSLLQVSA NDCDSGENAE ISYFTLTPDF TVSSHGIIFP ARQLDYERPY HSYEFVIMAV
DRGEVPKTGT ATVRIRMTNV NDEAPEFSQA IYRTFVSEDA GPHTLIATVH AIDSDGDGVS
YKIVAGNEEG NFVTDYQKGI IRLRSTPPPR LQGTEYVLNI TATDDNSSGG LHSLSSTALV
IVGVDDVNNN KPIFQKCQYY RDHASVLENQ PSETFVLQVE ASDADEGANG RVKYGIMHRD
GALLGFHIHP DTGILTTALR FDRELQREYP ITVTATDQAT EPLIGICQMN IQILDENDND
PKFENTRYEY FLKEDTPVGT SFLRVAAHDD DYGINAAITY SMSAEASEYF KVNPVTGWVS
VNQPISQRSY ITHEIIATDG GNRSTRVELS VTITNVKNQP LHWEKETYEV VIPENTTRDT
PIVIIKATSL LGDPRVTYNL EEGLVPETNM PVRFYLMPNR EDGSASILVA EPLDFETTRS
FVLKVRAQNV AVVPLAAFAT VHVNVTDVND NVPFFTSSIY EASVTEGTEI GTVVIQVSAT
DLDLGENGKI TYSLLNDLNG DHQFFQIEAT TGLIYCETVF DREVKRSYLL EVKSTDGSES
ARPGKHGQPN YDTAYVRIFI TDVNDNKPMF SQSVYEVTVD EDQDVNFPVI TVSANDEDEG
ANAKLKYQIT SGNIGGMFDV EPEVGTIFIS QKLDYEETKQ YELHLVASDG KWEDYVTVIV
HVINKNDEAP FFSVNEYYGS VTEELDGSPV FVLQVTAVDP DTYADYGTLK YSLHGQGADC
EFKIDENTGN IYSQKTLDRE ERAVWRFVVL ATDEGGEGLT GFTDVIINVQ DINDNSPIFT
CNPDNCHGNV FENSPADTSI MEMIASDRDD TNIGHNAILT YNIIENAKND INLDLFHINP
KTGTIYVALG TLDREKTDKY FLLVEAKDGG GLTGTATATI WVSDINDHAP KFAKPLWKAK
ISEHSELNSE ILIVTATDAD TGENAQLTFT IINGDPEQKF YIENHIKGQH GTIKLNKRLD
FEKPHERWFN LTIKVEDLDF SSVAHCLIEV EDYNDNSPVF TPHFHHVSPV FENAPIGSTV
AKVVATDIDS GLNGKILYSI QSDSDPFGQF TIDQAGYVTV ANTLDREIMQ QYNLIILARD
EGVPSQTGSA TVLLTLIDIN DNGPTFEVAY MPVVCENVQG PQIVHVNETS LLIYAVDRDT
VENGQPFSFA LAPEYKNSFD FTLKDNSNNT ATVTALRPFD REEQKEYYFP IVITDSGSPP
MSATNTLTIT IGDENDHPHL AGHKEIYVNN IKGKLAAIML GKIHAPDPDE WDNKTYIFEG
YVPKYFILNQ RTGFLLIKGT TPQGTYNFKV RVSDGIWPDA ISTVKVHVKE LTDEAIYNSG
SLRLADITAD EFIQKGEDGK SRYDRFKKLL SEIFSAPQSK INIFSVMNTK NRQTDIRFSI
YSSLHYRAER LNGNVAAHSK RLQSSLKVNI SQIHIDECTR KKCTKNPGCT NYLVVSDLPT
AVDTGNISFV SVTVSVKAVC TCSAREQIHQ SCTSYPGNPC HNGGTCIDTQ NGYRCQCSSE
FEGPDCQRTK HTFHGNGYAW FPPFRPCFDS HLSLEFITEV PDGLLLYSGP ISDLGAGDKE
DFIAIELTDG IPVLKINHGS GTLVLRFPDS VNVADRKWHH LDVRSNGQVV YFTLDHCSST
VNSEKEGRGK LLSTKDRSAC EVTGSTPEEE SSSTFLNANL VLQLGGVKES IPYFYPQLQH
KHFTGCLRNL VLDTKVYDLG FPAESLNSFP GCKRTDWNCI SKGSPHCGVH GKCHGEWDSF
TCQCLPGYYG RQCEKAVKEY SFESGSHILY RLDGLLQGGR TQLQTMIRTR STNSVIMSIF
SRDTEHVTLE VAHGCLGVSY NYGNEDHTVK LASHRIDNGE WHLLTLDHIG REFTLRINRG
GGKREVTEML AQYMEIITNA STLLLGNIHP TSHNSFQGCL KDVRLNNYQV PLDAKSKDLV
SVVSSAGVSE GCSSQACEND PCRKPFLCVD LWRMYECRCP SGHLAVENAT GKTCVYTLCA
NQPCHHGICV AQSPQNIICH CQEGYTGRHC EVTLAIYRDD LGLSFTSMFA ICVCFLALLV
LLSGVLLWTR WRNYQGLKEG IYHASAHHDD WEDIRENVLD YDEEGGGEQD HDAYNMSELQ
MSLQASPTPS VNRKTQHGNM PPSHKQLKLS ASKRSSSFTS EDFAHYLSDI VRNVDRDPQA
LPSDSLKVYL TEGEGSLVAS LSSLGSSALD ENVNYNYTDE WGPKFDQIKA LCKHSNRNS
//
