ID A0A1S3FSE1_DIPOR Unreviewed; 1111 AA.
AC A0A1S3FSE1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Neuronal cell adhesion molecule isoform X9 {ECO:0000313|RefSeq:XP_012879483.1};
GN Name=Nrcam {ECO:0000313|RefSeq:XP_012879483.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012879483.1};
RN [1] {ECO:0000313|RefSeq:XP_012879483.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012879483.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000256|ARBA:ARBA00008588}.
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DR RefSeq; XP_012879483.1; XM_013024029.1.
DR AlphaFoldDB; A0A1S3FSE1; -.
DR GeneID; 105991393; -.
DR CTD; 4897; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR CDD; cd05868; Ig4_NrCAM; 1.
DR CDD; cd05874; IgI_NrCAM; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
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; IPR003006; Ig/MHC_CS.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR44170:SF15; NEURONAL CELL ADHESION MOLECULE; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 3.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS00290; IG_MHC; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1111
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010288089"
FT TRANSMEM 1051..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..128
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 135..229
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 261..350
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 355..442
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 448..535
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 539..626
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 633..728
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 730..827
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 832..934
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 938..1034
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1081..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 123637 MW; 787A6CCC6C52DE64 CRC64;
MQLKIMPKKK RLSAGRVPLI LFLCQMISAL EVPLDLVQPP TITQQSPKDY IIDPRENIVI
QCEAKGKPPP SFSWTRNGTH FDIDKDPLVT MKTGSGTLII NIMSEGKAET YEGVYQCTAR
NERGAAISNN IVIRPSRSPL WTKEKLEPII LQNGQPLVLP CRPPIGLPPA IIFWMDNSFQ
RLPQSERVSQ GLNGDLYFSN VLPEDTREDY ICYARFNHTQ TIQQKQPISV KVISVDELND
TLAANLSDTE FYSAKSSRER PPTFLTPEGN ASRKEELRGN VLSLECIAEG LPTPIIYWIK
EDGILPVNRT FYRNFKKTLQ ITHVSEADSG NYQCIAKNPL GAIHHTISVT VKAAPYWIVA
PQNLVLSPGE DGSLICRANG NPKPRISWLT NGVPIEIAPD DPSRKIDGDT IIFSNVQERS
SAVYQCNASN EYGYLLANAF VNVLAEPPRI LTSANTLYQV IANRPALLDC AFFGSPLPTI
EWFKGAKGRA LHEDIYILHE NGTLEIPVAQ KDSTGTYTCV ARNKLGMAKN EVHLEIKDPT
RIIKQPEYAI VQRGSTVSFE CKVKHDHTLI PTVMWLKDNG ELPSDERFTV DKDHLVVTDV
DDRDGGTYTC VANTTLDKVS ASAVLSVVDV PNPPIDLELT NQLDKSVQLT WTPGDDNNSP
ITKFIIEYED TMHEAGLWHH QAEVPGTQTT AQLKLSPYVN YSFRVTAVNN IGQSLPSEAS
EQYFTKAAEP DKNPTDVEGL GSEPDNLVIT WKPLNGFESN GPGLQYKVSW RQKDGDDEWT
SVLVANVSKY IVSGTPTFVP YLIKVQALND VGFAPEPAEV MGHSGEDLPM VAPGNVHVNV
VNSTLAEVHW DPVPLKSIRG HLQGYRIYYW KAHSSSRRDK RHIEKKILTF QGSKTHGMLP
GLEPFSHYAL NVRVVNGKGE GPASPDRVFH TPEGVPSAPS SLKIINPSLD SLTLEWDPPS
HPNGILTEYT LKYQPINSTH ELGPLLDLKI PANKTRWILK NLNFSTRYKF YFYAHTSAGP
GSHITEEAIT TMDAGKMAMA SRQVDIATQG WFIGLMCAVA LLILILLIVC FIRRNKGGKY
PVKEKEDAHA DPEIQPMKED DGTFGEYRRK T
//
