ID A0A452HPY1_9SAUR Unreviewed; 2307 AA.
AC A0A452HPY1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Neural-cadherin-like {ECO:0008006|Google:ProtNLM};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000017069.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000017069.1}
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; 38772.ENSGAGP00000017069; -.
DR Ensembl; ENSGAGT00000019480.1; ENSGAGP00000017069.1; ENSGAGG00000012743.1.
DR Proteomes; UP000291020; 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; 12.
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; 12.
DR Gene3D; 2.10.25.10; Laminin; 2.
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:SF442; DACHSOUS CADHERIN-RELATED 2; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 10.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 13.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 13.
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; 6.
DR PROSITE; PS50268; CADHERIN_2; 12.
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:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..2307
FT /note="Neural-cadherin-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019532702"
FT TRANSMEM 2111..2131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..105
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 106..212
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 224..321
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 322..421
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 422..533
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 534..648
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 649..750
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 751..857
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 861..971
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 972..1079
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1081..1185
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1185..1299
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1549..1588
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1589..1790
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1793..1832
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1835..2012
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2057..2094
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 1578..1587
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1822..1831
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2084..2093
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2307 AA; 255946 MW; 1A2839013A9B3CF7 CRC64;
MMHCGTFFHG KLMSLGSVKI FLFFLVLATD CDSGSNAEIT YFIQSTDFSI TPEGVISSHQ
QLNFERANHM YEFVVIAVDK GHHPQTGTAS VRIRMTNVND EAPVFSQSGY KTFLSEDAGP
STLVAAVHAK DPDGDGVLYQ IAGGNEDGNF ELDGQKGIIK LRRNPVPKLK GPRYILNITA
IDDNASGGPA PLSSFAVVIV GINDINNNKP VFRKCTDYSD STWILENQPP GTYVLQVEAY
DADLGLNGEV KYGLMHRDGA SPGFSIDPDT GIITTTQSFD REKLRECMLS VTATDQAQEP
LIGVCQITIF IADVNDNDPK FENSRYQYFL REDTPVGTSF LRAAAHDDDQ GVNAAIVYSM
LQQQPEYFQI NPSTGWVYVN HLISQTTRIS RYIVATDGGN RSSTVELTVT ITNILNQPPH
WEQSGYWATI PENTIRDTNI MTVKATSSLG DPRVTYNLEE GQVPETNMPI RFYLKPNRVD
GSASLLVSEP LDFETTKFFT LRVRAQNVAM IPLASFTTVC INITDVNDNV PFFTSSTYKV
SVPEEAAIGT SVAQVLATDL DSGPHGEVQY SILKDFSEDY QFFTIHPETG IISTKASFDR
EKKGSYLIEV QSQDSAESAR PGVYGQPNTD TAYVKIFVSD VNDNAPAFPH PVYEISIEED
KEVGYAIVTV TANDEDEGAN AKLRYQITSG NVKGAFDVEP ELGTIFITQC LDYEQEQRYE
LRIVASDGKW ENHTLVAISV INKNDESPVF TNNEYHASVL EELTDLPVLV LKVSATDPDQ
EADQSALCYS LHGHGANSEF CINKYTGEIY ANKKLDREKR SMWRFLVLAT DENGEGLTGF
ADVIIEVRDV NDNPPLFLCM SEGCFVGQVP EDSPADTTVM EMNAIDLDDP KTGKNAVLTY
RIIQNVQNEI NLNLFSINPV MGTICTVLGS LDREKENKYL VVVEGRDGGG LTGTGTATIL
VSDINDHAPV FTRKMYTAFV SENASINTEI TMVSAMDRDE GENAVVTFSI LDGDDDCKFS
IETDKINKRG AIRLRKHLDF EKPHERMFNL TVKAEDTDFF SIAHCVIYVE DSNDHAPVFY
PPFYEVMALA EDVPLGTRVV QVSAVDLDSG LNGRFLYRLI NRSDPSGQFS VGNDGWVVVA
GLLDHETVTQ HHLVVIATDM GQPRLTGSAT VLVTLQDVND NGPEFEAQYN PVVWENTASP
QIVQMNETST LLYARDRDTA ANGGPFSFHL LSNFGSVTYF NLQDFSNGSA LLTALHTFDR
EVHKVFYLPI LITDSGIPPM SSTNTLTVHI GDRNDHPHSA GYMECLIYCY DGILPTTVLG
QVHAPDHDDW DHKTYQFEEK ASRYFILNHN SGLLSIKEGT PTGIYNVRVK VTDGIWPDVI
STVKVVVKEI KDDAIRNAGS IRINDITAED FIFQSSERES KYNQMKKLLS EIIPAQLENV
HIFSVLNTPG QTRVVDVWFT VSGPPYYKAE KLNGNVAVSK ARLEIILNIN ITQIGIDGCV
TANCTHSTGC VSKYNYSHVP TITTAGSVSL ASVTVLNSAQ CTCAARESQH LFCSSYRTNP
CLNGGTCIDT DLGYSCKCPA TFDGPDCQQT KRTFRGHGYA WFPPIKPCFE SRISLEFITD
VTDGLLLYNG PLAHGHPGEV EDFIALELSD SVPSLTLSHG SGVLFLQLSQ KVNVADRRWH
NIKIISDGKK VQLILDHCVN VSVKDDDGIR KEISQMDLSA CEVSEETPGN ERFLNVHQPL
QLGGVKKALP YRNSQKHFKG FVGCIRNVII DSKVYDLEHP AESLNSVPGC TMTDEMCHRA
GVLSCGIHGK CIGEWGSFNC GCYPGYAGSK CTKVLLEWAF GRNSWIHYEL KSFLSAHVTQ
VQLMVRTRVS FSTLLSMASA DGSRYIRLEV VDGHFGVNFN LEDKEQRLRL STLRIDNGQW
VLLTMERYNN EFTLRVNNGG GDHEMTSFMG ANRWFKMDLA SIVLGNHVPN HSESDFQGCM
RDVQLNGQPL LGDDKSTEFS FILKQQGITI GCHSNACRSQ PCHSPFHCVD LWRRHECRCP
TGKVEVTDNL TGLKHCTSTP CGLWNCRNGG TCVTHSQDKF VCQCPDGYKG KWCEISQVKA
GKPVGLSSGS ILAISMCLLV FLALLVSYTV WSQWGRSGFR KGGVYHIPEE HESWEDVREN
VFNYNEEGGG EHDQTAYDID ELKKPLQSIP QFSSETTAPH FKTHFCPERD PFTKHSHQRD
SNSAVTSISD FKEYVSQIIY DADNDLRSLP ADTVHFYCLE GQCSLAGSLS SLDSSSVDED
LNYNDLHEWG SKFDKLKELY ALSNEHL
//
