MDGA1_CHICK
ID MDGA1_CHICK Reviewed; 949 AA.
AC Q0WYX8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=MAM domain-containing glycosylphosphatidylinositol anchor protein 1;
DE Flags: Precursor;
GN Name=MDGA1 {ECO:0000312|EMBL:BAE98269.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE98269.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryonic spinal cord {ECO:0000269|PubMed:16782075};
RX PubMed=16782075; DOI=10.1016/j.brainres.2006.05.030;
RA Fujimura Y., Iwashita M., Matsuzaki F., Yamamoto T.;
RT "MDGA1, an IgSF molecule containing a MAM domain, heterophilically
RT associates with axon- and muscle-associated binding partners through
RT distinct structural domains.";
RL Brain Res. 1101:12-19(2006).
CC -!- FUNCTION: Required for radial migration of cortical neurons in the
CC superficial layer of the neocortex. {ECO:0000250|UniProtKB:Q0PMG2}.
CC -!- SUBUNIT: Interacts heterophilically through its MAM domain with
CC proteins in axon-rich regions and through its Ig-like domains with
CC proteins in differentiating muscle. {ECO:0000269|PubMed:16782075}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16782075};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:16782075}. Note=Associated
CC with lipid rafts. {ECO:0000250|UniProtKB:Q8NFP4,
CC ECO:0000269|PubMed:16782075}.
CC -!- TISSUE SPECIFICITY: In the embryonic brachial spinal cord, selectively
CC expressed by medial lateral motor column neurons, some populations of
CC dorsal root ganglion neurons, and interneurons.
CC {ECO:0000269|PubMed:16782075}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB241390; BAE98269.1; -; mRNA.
DR RefSeq; NP_001038112.1; NM_001044647.1.
DR PDB; 5OJ2; X-ray; 3.20 A; A/B=19-919.
DR PDB; 5OJ6; X-ray; 3.30 A; B=19-919.
DR PDBsum; 5OJ2; -.
DR PDBsum; 5OJ6; -.
DR AlphaFoldDB; Q0WYX8; -.
DR SMR; Q0WYX8; -.
DR STRING; 9031.ENSGALP00000016475; -.
DR PaxDb; Q0WYX8; -.
DR GeneID; 421431; -.
DR KEGG; gga:421431; -.
DR CTD; 266727; -.
DR VEuPathDB; HostDB:geneid_421431; -.
DR eggNOG; ENOG502QUWH; Eukaryota.
DR InParanoid; Q0WYX8; -.
DR PhylomeDB; Q0WYX8; -.
DR PRO; PR:Q0WYX8; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR CDD; cd06263; MAM; 1.
DR DisProt; DP02619; -.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF00629; MAM; 1.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS50060; MAM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW Lipoprotein; Membrane; Neurogenesis; Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..926
FT /note="MAM domain-containing glycosylphosphatidylinositol
FT anchor protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000292930"
FT PROPEP 927..949
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000292931"
FT DOMAIN 24..125
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 132..230
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 240..323
FT /note="Ig-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 338..432
FT /note="Ig-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 440..531
FT /note="Ig-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 537..625
FT /note="Ig-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 637..737
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 745..912
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT LIPID 926
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 262..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 357..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 463..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 559..609
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 23..34
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5OJ6"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:5OJ2"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 118..129
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 146..158
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 193..203
FT /evidence="ECO:0007829|PDB:5OJ2"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:5OJ2"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 258..269
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:5OJ2"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 329..337
FT /evidence="ECO:0007829|PDB:5OJ2"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 353..361
FT /evidence="ECO:0007829|PDB:5OJ2"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 367..375
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 383..396
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:5OJ2"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 411..419
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 464..469
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 491..502
FT /evidence="ECO:0007829|PDB:5OJ2"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 509..515
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 527..541
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 555..566
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 591..598
FT /evidence="ECO:0007829|PDB:5OJ2"
FT TURN 601..603
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 605..612
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 617..625
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 649..659
FT /evidence="ECO:0007829|PDB:5OJ2"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 669..675
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 683..688
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 698..708
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 711..719
FT /evidence="ECO:0007829|PDB:5OJ2"
FT STRAND 727..731
FT /evidence="ECO:0007829|PDB:5OJ2"
SQ SEQUENCE 949 AA; 106025 MW; 0D10DB4DAE724B87 CRC64;
MEMICVLFLS LVPAYSRGQG VYAPAQAQII HAGQACVVKE DNISERVYTI REGDTLVLQC
LVTGHPRPQV RWTKTAGSAS DKFQETSVLN ETLRIEKIQR LQGGRYYCKA ENGVGVPAIR
SIRVDVQYLD EPVLTVHQTI SDVRGSFYQE KTVFLRCTVN SNPPARFIWK RGAETLSHSQ
DNGVDIYEPL YTQGETKVLK LKNLRPQDYA SYTCQVSVRN VCSIPDKSIT FQLTNTTAPP
ALKLSVNETL VVNPGDNVTM QCSLTGGDPQ PEVLWSHSPG PLPPNSLVQG GNLTIWRIRV
EDSGYYNCTA INNVGNPAKK TVNLLVRSMK NATFQITPDV IKESETIQLG QDLKLSCHVD
AVPQEKVVYS WYKNGKPARF SDRLLITRND PELPPVTCSL EIIDLRFSDY GTYLCVATFQ
GAPIPDLSVE VNISSETVPP TISVPKGQST ITVREGSRAE LQCEVRGKPK PPIIWSRVDK
ETPMPSGTMT VETYDGKLRL ESVSRDMSGT YKCQTARYNG FNIRPREALV QLNVQFPPVV
EPAFQDVRQG MGRSVTLRCT MLKGSPMKVA TSVWRFNGTL LAQPPAEQQD YSELKVDSVS
RETSGSYECS ISNDVGVSAC LFQVSAKAYS PEFYYDTPNP TLSQKQSKNY SYILQWTQKE
PDAVDPILKY RLEVRQLAQR NTIQTFIPVQ KMEKGLLLEH ILPNLKVPQS YEVRLTPITS
FGAGDMAARI IRYMEPINYP SPTDNTCRFE DEKICGFVQD KMDNFDWTRQ NALTQNPKRT
VNTGPPTDIS GTPEGYYMFI EASRPRVTGD KARLISPLYN ITAKYYCVSF YYHMYGKHIG
SLNLLVRVRN KRAIDTQVWS LSGNRGNMWQ QAHVPINPPG PFQIIFEGVR GTSYEGDIAI
DDVTLKKGDC PRKPIGPNKA VALPGSGVSA QHGPCLCGPL TFFLYVLLR
